The domain within your query sequence starts at position 1187 and ends at position 1452; the E-value for the PTPc domain shown below is 4.24e-98.
WARNING!
Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 98221181 ) for details.
Catalytic residues | |||
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Position | Amino acid | Present? | |
Domain | Protein | ||
169 | 1355 | D | No |
205 | 1391 | C | Yes |
249 | 1435 | Q | No |
QIKDEFQTLNIVTPRVRPEDCSIGLLPRNHDKNRSMDVLPLDRCLPFLISVDGESSNYIN AALMDSHKQPAAFVVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDTAQLCMQYWPEKTS GCYGPIQVEFVSADIDEDIIHRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSL LKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHIVKTL RNNKSNMVETLEQYKFVYEVALEYLS
PTPcProtein tyrosine phosphatase, catalytic domain |
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SMART accession number: | SM00194 |
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Description: | - |
Interpro abstract (IPR000242): | Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48 ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [ (PUBMED:9818190) (PUBMED:14625689) ]. The PTP superfamily can be divided into four subfamilies [ (PUBMED:12678841) ]:
Based on their cellular localisation, PTPases are also classified as:
All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif [ (PUBMED:9646865) ]. Functional diversity between PTPases is endowed by regulatory domains and subunits. This entry represents the PTPase domain found in several tyrosine-specific protein phosphatases (PTPases). Structurally, all known receptor PTPases, are made up of a variable length extracellular domain, followed by a transmembrane region and a C-terminal catalytic cytoplasmic domain. Some of the receptor PTPases contain fibronectin type III (FN-III) repeats, immunoglobulin-like domains, MAM domains or carbonic anhydrase-like domains in their extracellular region. The cytoplasmic region generally contains two copies of the PTPase domain. The first seems to have enzymatic activity, while the second is inactive. The inactive domains of tandem phosphatases can be divided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. There is a region of higher conservation common to both classes, suggesting a new regulatory centre [ (PUBMED:14739250) ]. PTPase domains consist of about 300 amino acids. There are two conserved cysteines, the second one has been shown to be absolutely required for activity. Furthermore, a number of conserved residues in its immediate vicinity have also been shown to be important. |
GO process: | protein dephosphorylation (GO:0006470) |
GO function: | protein tyrosine phosphatase activity (GO:0004725) |
Family alignment: |
There are 37989 PTPc domains in 29134 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Taxonomic distribution of proteins containing PTPc domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with PTPc domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing PTPc domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
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Cellular role: signalling
Binding / catalysis: protein tyrosine phosphatase - Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Hofmann K, Bucher P, Kajava AV
- A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain.
- J Mol Biol. 1998; 282: 195-208
- Display abstract
Mammalian Cdc25 phosphatase is responsible for the dephosphorylation of Cdc2 and other cyclin-dependent kinases at Thr14 and Tyr15, thus activating the kinase and allowing cell cycle progression. The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. Apart from a CX3R motif, which is present at the active site of all known tyrosine phosphatases, Cdc25 does not share any obvious sequence similarity with any of those enzymes. Until very recently, the Cdc25 family was the only subfamily of tyrosine phosphates for which no three-dimensional structural data were available. Using the generalized profile technique, a sensitive method for sequence database searches, we found an extended and highly significant sequence similarity between the Cdc25 catalytic domain and similarly sized regions in other proteins: the non-catalytic domain of two distinct families of MAP-kinase phosphates, the non-catalytic domain of several ubiquitin protein hydrolases, the N and C-terminal domain of rhodanese, and a large and heterogeneous groups of stress-response proteins from all phyla. The relationship of Cdc25 to the structurally well-characterized rhodanese spans the entire catalytic domain and served as template for a structural model for human Cdc25a, which is fundamentally different from previously suggested models for Cdc25 catalytic domain organization. The surface positioning of subfamily-specific conserved residues allows us to predict the sites of interaction with Cdk2, a physiological target of Cdc25a. Based on the results of this analysis, we also predict that the budding yeast arsenate resistance protein Acr2 and the ORF Ygr203w encode protein phosphatases with catalytic properties similar to that of the Cdc25 family. Recent determination of the crystal structure of the Cdc25a catalytic domain supports the validity of the model and demonstrates the power of the generalized sequence profile technique in homology-based modeling of the three-dimensional structure of a protein having a weak but significant sequence similarity with a structurally characterized protein.
- VanVactor D
- Protein tyrosine phosphatases in the developing nervous system.
- Curr Opin Cell Biol. 1998; 10: 174-81
- Display abstract
Protein tyrosine phosphatases (PTPs) constitute a diverse family of intracellular and transmembrane proteins. Expression data and recent genetic analyses indicate that many PTPs play important roles in different aspects of nervous system development. Although PTP mechanisms are still poorly understood, current data suggest considerable complexity in these signaling pathways.
- Zhang ZY
- Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.
- Crit Rev Biochem Mol Biol. 1998; 33: 1-52
- Display abstract
The protein-tyrosine phosphatases (PTPases) superfamily consists of tyrosine-specific phosphatases, dual specificity phosphatases, and the low-molecular-weight phosphatases. They are modulators of signal transduction pathways that regulate numerous cell functions. Malfunction of PTPases have been linked to a number of oncogenic and metabolic disease states, and PTPases are also employed by microbes and viruses for pathogenicity. There is little sequence similarity among the three subfamilies of phosphatases. Yet, three-dimensional structural data show that they share similar conserved structural elements, namely, the phosphate-binding loop encompassing the PTPase signature motif (H/V)C(X)5R(S/T) and an essential general acid/base Asp residue on a surface loop. Biochemical experiments demonstrate that phosphatases in the PTPase superfamily utilize a common mechanism for catalysis going through a covalent thiophosphate intermediate that involves the nucleophilic Cys residue in the PTPase signature motif. The transition states for phosphoenzyme intermediate formation and hydrolysis are dissociative in nature and are similar to those of the solution phosphate monoester reactions. One strategy used by these phosphatases for transition state stabilization is to neutralize the developing negative charge in the leaving group. A conformational change that is restricted to the movement of a flexible loop occurs during the catalytic cycle of the PTPases. However, the relationship between loop dynamics and enzyme catalysis remains to be established. The nature and identity of the rate-limiting step in the PTPase catalyzed reaction requires further investigation and may be dependent on the specific experimental conditions such as temperature, pH, buffer, and substrate used. In-depth kinetic and structural analysis of a representative number of phosphatases from each group of the PTPase superfamily will most likely continue to yield insightful mechanistic information that may be applicable to the rest of the family members.
- Frearson JA, Alexander DR
- The role of phosphotyrosine phosphatases in haematopoietic cell signal transduction.
- Bioessays. 1997; 19: 417-27
- Display abstract
Phosphotyrosine phosphatases (PTPases) are the enzymes which remove phosphate groups from protein tyrosine residues. An enormous number of phosphatases have been cloned and sequenced during the past decade, many of which are expressed in haematopoietic cells. This review focuses on the biochemistry and cell biology of three phosphatases, the transmembrane CD45 and the cytosolic SH2-domain-containing PTPases SHP-1 and SHP-2, to illustrate the diverse ways in which PTPases regulate receptor signal transduction. The involvement of these and other PTPases has been demonstrated in haematopoietic cell development, apoptosis, activation and nonresponsiveness. A common theme in the actions of many haematopoietic cell PTPases is the way in which they modulate the thresholds for receptor signalling, thereby regulating critical events in the positive and negative selection of lymphocytes. There is growing interest in haematopoietic PTPases and their associated regulatory proteins as targets for pharmaceutical intervention and in the involvement of these enzymes in human disease.
- Neel BG, Tonks NK
- Protein tyrosine phosphatases in signal transduction.
- Curr Opin Cell Biol. 1997; 9: 193-204
- Display abstract
Protein-tyrosyl phosphorylation, regulated by protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is a key cellular control mechanism. Until recently, little was known about PTPs. However, the past two years have witnessed an explosion of information about PTP structure, regulation and function. Crystal structures of several PTPs have provided insights into enzymatic mechanisms and regulation and suggested the design of 'substrate-trapping' mutants. Candidate homophilic and heterophilic ligands for transmembrane PTPs have been identified, and roles for transmembrane PTPs in regulating cell-cell interactions have been suggested. Finally, progress has been made in understanding signaling by Src homology 2 domain containing PTPs and PTPs controlling yeast osmoregulatory pathways.
- Takagi T, Moore CR, Diehn F, Buratowski S
- An RNA 5'-triphosphatase related to the protein tyrosine phosphatases.
- Cell. 1997; 89: 867-73
- Display abstract
mRNA capping requires the sequential action of three enzymatic activities: RNA triphosphatase, guanylyl-transferase, and methyltransferase. Here we characterize a gene (CEL-1) believed to encode the C. elegans capping enzyme. CEL-1 has a C-terminal domain containing motifs found in yeast and vaccinia virus capping enzyme guanylyltransferases. The N-terminal domain of CEL-1 has RNA triphosphatase activity. Surprisingly, this domain does not resemble the vaccinia virus capping enzyme but does have significant sequence similarity to the protein tyrosine phosphatase (PTP) enzyme family. However, CEL-1 has no detectable PTP activity. The mechanism of the RNA triphosphatase is similar to that of PTPs: the active site contains a conserved nucleophilic cysteine required for activity. These results broaden the superfamily of PTP-like phosphatases to include enzymes with RNA substrates.
- Zhang ZY
- Structure, mechanism, and specificity of protein-tyrosine phosphatases.
- Curr Top Cell Regul. 1997; 35: 21-68
- Fauman EB, Saper MA
- Structure and function of the protein tyrosine phosphatases.
- Trends Biochem Sci. 1996; 21: 413-7
- Display abstract
The tyrosine and dual-specificity phosphatases are involved in signaling, cell growth and differentiation, and the cell cycle. The enzymes share a common catalytic mechanism mediated by an active site cysteine, arginine and aspartic acid. Supplementary domains assist in targeting and substrate specificity.
- Tonks NK, Neel BG
- From form to function: signaling by protein tyrosine phosphatases.
- Cell. 1996; 87: 365-8
- Barford D, Jia Z, Tonks NK
- Protein tyrosine phosphatases take off.
- Nat Struct Biol. 1995; 2: 1043-53
- Display abstract
Protein tyrosine phosphatases (PTPs) are a family of signal transduction enzymes that dephosphorylate phosphotyrosine containing proteins. Structural and kinetic studies provide a molecular understanding of how these enzymes regulate a wide range of intracellular processes.
- Jia Z, Barford D, Flint AJ, Tonks NK
- Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B.
- Science. 1995; 268: 1754-8
- Display abstract
The crystal structures of a cysteine-215-->serine mutant of protein tyrosine phosphatase 1B complexed with high-affinity peptide substrates corresponding to an autophosphorylation site of the epidermal growth factor receptor were determined. Peptide binding to the protein phosphatase was accompanied by a conformational change of a surface loop that created a phosphotyrosine recognition pocket and induced a catalytically competent form of the enzyme. The phosphotyrosine side chain is buried within the period and anchors the peptide substrate to its binding site. Hydrogen bonds between peptide main-chain atoms and the protein contribute to binding affinity, and specific interactions of acidic residues of the peptide with basic residues on the surface of the enzyme confer sequence specificity.
- Zondag GC, Koningstein GM, Jiang YP, Sap J, Moolenaar WH, Gebbink MF
- Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain.
- J Biol Chem. 1995; 270: 14247-50
- Display abstract
The receptor-like protein tyrosine phosphatases (RPTP) mu and RPTP kappa have a modular ectodomain consisting of four fibronectin type III-like repeats, a single Ig-like domain, and a newly identified N-terminal MAM domain. The function of the latter module, which comprises about 160 amino acids and is found in diverse transmembrane proteins, is not known. We previously reported that both RPTP mu and RPTP kappa can mediate homophilic cell interactions when expressed in insect cells. Here we show that despite their striking structural similarity, RPTP mu and RPTP kappa fail to interact in a heterophilic manner. To examine the role of the MAM domain in homophilic binding, we expressed a mutant RPTP mu lacking the MAM domain in insect Sf9 cells. Truncated RPTP mu is properly expressed at the cell surface but fails to promote cell-cell adhesion. Homophilic cell adhesion is fully restored in a chimeric RPTP mu molecule containing the MAM domain of RPTP kappa. However, this chimeric RPTP mu does not interact with either RPTP mu or RPTP kappa. These results indicate that the MAM domain of RPTP mu and RPTP kappa is essential for homophilic cell-cell interaction and helps determine the specificity of these interactions.
- Barford D, Flint AJ, Tonks NK
- Crystal structure of human protein tyrosine phosphatase 1B.
- Science. 1994; 263: 1397-404
- Display abstract
Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation.
- Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA
- Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate.
- Nature. 1994; 370: 571-5
- Display abstract
Protein tyrosine phosphatases (PTPases) and kinases coregulate the critical levels of phosphorylation necessary for intracellular signalling, cell growth and differentiation. Yersinia, the causative bacteria of the bubonic plague and other enteric diseases, secrete an active PTPase, Yop51, that enters and suppresses host immune cells. Though the catalytic domain is only approximately 20% identical to human PTP1B, the Yersinia PTPase contains all of the invariant residues present in eukaryotic PTPases, including the nucleophilic Cys 403 which forms a phosphocysteine intermediate during catalysis. We present here structures of the unliganded (2.5 A resolution) and tungstate-bound (2.6 A) crystal forms which reveal that Cys 403 is positioned at the centre of a distinctive phosphate-binding loop. This loop is at the hub of several hydrogen-bond arrays that not only stabilize a bound oxyanion, but may activate Cys 403 as a reactive thiolate. Binding of tungstate triggers a conformational change that traps the oxyanion and swings Asp 356, an important catalytic residue, by approximately 6 A into the active site. The same anion-binding loop in PTPases is also found in the enzyme rhodanese.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 20.43 map04520 Adherens junction 10.22 map04010 MAPK signaling pathway 9.14 map04650 Natural killer cell mediated cytotoxicity 8.60 map05120 Epithelial cell signaling in Helicobacter pylori infection 8.60 map04514 Cell adhesion molecules (CAMs) 8.06 map04660 T cell receptor signaling pathway 6.45 map04940 Type I diabetes mellitus 6.45 map04910 Insulin signaling pathway 4.84 map04662 B cell receptor signaling pathway 4.30 map05211 Renal cell carcinoma 4.30 map05220 Chronic myeloid leukemia 4.30 map04920 Adipocytokine signaling pathway 4.30 map04670 Leukocyte transendothelial migration This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with PTPc domain which could be assigned to a KEGG orthologous group, and not all proteins containing PTPc domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of PTPc domains in PDB
PDB code Main view Title 1a5y PROTEIN TYROSINE PHOSPHATASE 1B CYSTEINYL-PHOSPHATE INTERMEDIATE 1aax CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH TWO BIS(PARA-PHOSPHOPHENYL)METHANE (BPPM) MOLECULES 1bzc HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI 1bzh Cyclic peptide inhibitor of human PTP1B 1bzj Human ptp1b complexed with tpicooh 1c83 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 6-(OXALYL-AMINO)-1H-INDOLE-5-CARBOXYLIC ACID 1c84 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 3-(OXALYL-AMINO)-NAPHTHALENE-2-CARBOXLIC ACID 1c85 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO)-BENZOIC ACID 1c86 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B (R47V,D48N) COMPLEXED WITH 2-(OXALYL-AMINO-4,7-DIHYDRO-5H-THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID 1c87 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO-4,7-DIHYDRO-5H-THIENO[2,3-C]PYRAN-3-CARBOXYLIC ACID 1c88 CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 2-(OXALYL-AMINO)-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]PYRIDINE-3-CARBOXYLIC ACID 1ecv CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH 5-IODO-2-(OXALYL-AMINO)-BENZOIC ACID 1een CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH ACETYL-D-A-D-BPA-PTYR-L-I-P-Q-Q-G 1eeo CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH ACETYL-E-L-E-F-PTYR-M-D-Y-E-NH2 1fpr CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1. 1g1f CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE 1g1g CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A MONO-PHOSPHORYLATED PEPTIDE (ETDY(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE 1g1h CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A BIS-PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE 1g4u CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1 1g4w CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP 1g7f HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177496 1g7g HUMAN PTP1B CATALYTIC DOMAIN COMPLEXES WITH PNU179326 1gfy RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-TYROSINE PHOSPHATASE 1B AND ALPHA 1gwz CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTEIN TYROSINE PHOSPHATASE SHP-1 1i57 CRYSTAL STRUCTURE OF APO HUMAN PTP1B (C215S) MUTANT 1jf7 HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH PNU177836 1jln Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7 1kak Human Tyrosine Phosphatase 1B Complexed with an Inhibitor 1kav Human Tyrosine Phosphatase 1B Complexed with an Inhibitor 1l8g Crystal structure of PTP1B complexed with 7-(1,1-Dioxo-1H-benzo[d]isothiazol-3-yloxymethyl)-2-(oxalyl-amino)-4,7-dihydro-5H-thieno[2,3-c]pyran-3-carboxylic acid 1l8k T Cell Protein-Tyrosine Phosphatase Structure 1lar CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR 1lqf Structure of PTP1b in Complex with a Peptidic Bisphosphonate Inhibitor 1lyv High-resolution structure of the catalytically inactive yersinia tyrosine phosphatase C403A mutant in complex with phosphate. 1nl9 Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 12 Using a Linked-Fragment Strategy 1nny Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 23 Using a Linked-Fragment Strategy 1no6 Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 5 Using a Linked-Fragment Strategy 1nwe Ptp1B R47C Modified at C47 with N-[4-(2-{2-[3-(2-Bromo-acetylamino)-propionylamino]-3-hydroxy-propionylamino}-ethyl)-phenyl]-oxalamic acid 1nwl Crystal structure of the PTP1B complexed with SP7343-SP7964, a pTyr mimetic 1nz7 POTENT, SELECTIVE INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B USING A SECOND PHOSPHOTYROSINE BINDING SITE, complexed with compound 19. 1oem PTP1B with the catalytic cysteine oxidized to a sulfenyl-amide bond 1oeo PTP1B with the catalytic cysteine oxidized to sulfonic acid 1oes Oxidation state of protein tyrosine phosphatase 1B 1oet Oxidation state of protein tyrosine phosphatase 1B 1oeu Oxidation state of protein tyrosine phosphatase 1B 1oev Oxidation state of protein tyrosine phosphatase 1B 1ony Oxalyl-Aryl-Amino Benzoic Acid inhibitors of PTP1B, compound 17 1onz Oxalyl-aryl-Amino Benzoic acid Inhibitors of PTP1B, compound 8b 1p15 Crystal structure of the D2 domain of RPTPa 1pa1 Crystal structure of the C215D mutant of protein tyrosine phosphatase 1B 1pa9 Yersinia Protein-Tyrosine Phosphatase complexed with pNCS (Yop51,Pasteurella X,Ptpase,Yop51delta162) (Catalytic Domain, Residues 163-468) Mutant With Cys 235 Replaced By Arg (C235r) 1ph0 Non-carboxylic Acid-Containing Inhibitor of PTP1B Targeting the Second Phosphotyrosine Site 1ptt CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE-CONTAINING TETRA-PEPTIDE (AC-DEPYL-NH2) 1ptu CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE-CONTAINING HEXA-PEPTIDE (DADEPYL-NH2) 1ptv CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE 1pty CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH TWO PHOSPHOTYROSINE MOLECULES 1pxh Crystal structure of protein tyrosine phosphatase 1B with potent and selective bidentate inhibitor compound 2 1pyn DUAL-SITE POTENT, SELECTIVE PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR USING A LINKED FRAGMENT STRATEGY AND A MALONATE HEAD ON THE FIRST SITE 1q1m A Highly Efficient Approach to a Selective and Cell Active PTP1B inhibitors 1q6j THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 2 1q6m THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 3 1q6n THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 4 1q6p THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 6 1q6s THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 9 1q6t THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 11 1qxk Monoacid-Based, Cell Permeable, Selective Inhibitors of Protein Tyrosine Phosphatase 1B 1qz0 Crystal Structure of the Yersinia Pestis Phosphatase YopH in Complex with a Phosphotyrosyl Mimetic-Containing Hexapeptide 1rpm HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU, DOMAIN 1 1sug 1.95 A structure of apo protein tyrosine phosphatase 1B 1t48 Allosteric Inhibition of Protein Tyrosine Phosphatase 1B 1t49 Allosteric Inhibition of Protein Tyrosine Phosphatase 1B 1t4j Allosteric Inhibition of Protein Tyrosine Phosphatase 1B 1wax Protein tyrosine phosphatase 1B with active site inhibitor 1wch Crystal structure of PTPL1 human tyrosine phosphatase mutated in colorectal cancer - evidence for a second phosphotyrosine substrate recognition pocket 1xbo PTP1B complexed with Isoxazole Carboxylic Acid 1xxp Yersinia YopH (residues 163-468) C403S binds phosphotyrosyl peptide at two sites 1xxv Yersinia YopH (residues 163-468) binds phosphonodifluoromethyl-Phe containing hexapeptide at two sites 1yfo RECEPTOR PROTEIN TYROSINE PHOSPHATASE ALPHA, DOMAIN 1 FROM MOUSE 1ygr Crystal structure of the tandem phosphatase domain of RPTP CD45 1ygu Crystal structure of the tandem phosphatase domains of RPTP CD45 with a pTyr peptide 1ypt CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE 1ytn HYDROLASE 1yts A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA PROTEIN TYROSINE PHOSPHATASE 1ytw YERSINIA PTPASE COMPLEXED WITH TUNGSTATE 1zc0 Crystal structure of human hematopoietic tyrosine phosphatase (HePTP) catalytic domain 2a3k Crystal Structure of the Human Protein Tyrosine Phosphatase, PTPN7 (HePTP, Hematopoietic Protein Tyrosine Phosphatase) 2a8b Crystal Structure of the Catalytic Domain of Human Tyrosine Phosphatase Receptor, Type R 2ahs Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta 2azr Crystal structure of PTP1B with Bicyclic Thiophene inhibitor 2b07 Crystal structure of PTP1B with Tricyclic Thiophene inhibitor. 2b3o Crystal structure of human tyrosine phosphatase SHP-1 2b49 Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase, non-receptor Type 3 2b4s Crystal structure of a complex between PTP1B and the insulin receptor tyrosine kinase 2bgd Structure-based design of Protein Tyrosine Phosphatase-1B Inhibitors 2bge Structure-based design of Protein Tyrosine Phosphatase-1B Inhibitors 2bij Crystal structure of the human protein tyrosine phosphatase PTPN5 ( STEP, striatum enriched enriched Phosphatase) 2bv5 CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE PTPN5 AT 1.8A RESOLUTION 2bzl CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE N14 AT 1. 65 A RESOLUTION 2c7s Crystal structure of human protein tyrosine phosphatase kappa at 1. 95A resolution 2cfv Crystal structure of human protein tyrosine phosphatase receptor type J 2cjz crystal structure of the c472s mutant of human protein tyrosine phosphatase ptpn5 (step, striatum enriched phosphatase) in complex with phosphotyrosine 2cm2 Structure of Protein Tyrosine Phosphatase 1B (P212121) 2cm3 Structure of Protein Tyrosine Phosphatase 1B (C2) 2cm7 Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics 2cm8 Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics 2cma Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics 2cmb Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics 2cmc Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics 2cne Structural Insights into the Design of Nonpeptidic Isothiazolidinone- Containing Inhibitors of Protein Tyrosine Phosphatase 1B 2cnf Structural Insights into the Design of Nonpeptidic Isothiazolidinone- Containing Inhibitors of Protein Tyrosine Phosphatase 1B 2cng Structural Insights into the Design of Nonpeptidic Isothiazolidinone- Containing Inhibitors of Protein Tyrosine Phosphatase 1B 2cnh Structural Insights into the Design of Nonpeptidic Isothiazolidinone- Containing Inhibitors of Protein Tyrosine Phosphatase 1B 2cni Structural Insights into the Design of Nonpeptidic Isothiazolidinone- Containing Inhibitors of Protein Tyrosine Phosphatase 1B 2f6f The structure of the S295F mutant of human PTP1B 2f6t Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2f6v Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2f6w Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2f6y Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2f6z Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2f70 Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2f71 Protein tyrosine phosphatase 1B with sulfamic acid inhibitors 2fh7 Crystal structure of the phosphatase domains of human PTP SIGMA 2fjm The structure of phosphotyrosine phosphatase 1B in complex with compound 2 2fjn The structure of phosphotyrosine phosphatase 1B in complex with compound 2 2g59 Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo sapiens 2gjt Crystal structure of the human receptor phosphatase PTPRO 2gp0 HePTP Catalytic Domain (residues 44-339), S225D mutant 2h02 Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors 2h03 Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors 2h04 Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors 2h4g Crystal structure of PTP1B with monocyclic thiophene inhibitor 2h4k Crystal structure of PTP1B with a monocyclic thiophene inhibitor 2h4v Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma 2hb1 Crystal Structure of PTP1B with Monocyclic Thiophene Inhibitor 2hc1 Engineered catalytic domain of protein tyrosine phosphatase HPTPbeta. 2hc2 Engineered protein tyrosine phosphatase beta catalytic domain 2hnp CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B 2hnq CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B 2hvl Crystal structure of the HePTP catalytic domain C270S mutant 2hy3 Crystal structure of the human tyrosine receptor phosphate gamma in complex with vanadate 2i1y Crystal structure of the phosphatase domain of human PTP IA-2 2i3r Engineered catalytic domain of protein tyrosine phosphatase HPTPbeta 2i3u Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors 2i42 Crystal structure of Yersinia protein tyrosine phosphatase complexed with vanadate, a transition state analogue 2i4e Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors 2i4g Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with a sulfamic acid (soaking experiment) 2i4h Structural studies of protein tyrosine phosphatase beta catalytic domain co-crystallized with a sulfamic acid inhibitor 2i5x Engineering the PTPbeta catalytic domain with improved crystallization properties 2i75 Crystal Structure of Human Protein Tyrosine Phosphatase N4 (PTPN4) 2jjd Protein Tyrosine Phosphatase, Receptor Type, E isoform 2nlk Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase Gamma (D1+D2 PTPRG) 2nt7 Crystal structure of PTP1B-inhibitor complex 2nta Crystal Structure of PTP1B-inhibitor Complex 2nv5 Crystal structure of a C-terminal phosphatase domain of Rattus norvegicus ortholog of human protein tyrosine phosphatase, receptor type, D (PTPRD) 2nz6 Crystal structure of the PTPRJ inactivating mutant C1239S 2oc3 Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 18 2ooq Crystal Structure of the Human Receptor Phosphatase PTPRT 2p6x Crystal structure of human tyrosine phosphatase PTPN22 2pa5 Crystal structure of human protein tyrosine phosphatase PTPN9 2pbn Crystal structure of the human tyrosine receptor phosphate gamma 2pi7 Structure of the catalytic domain of the chick retinal neurite inhibitor-Receptor Protein Tyrosine Phosphatase CRYP-2/cPTPRO 2qbp Crystal structure of ptp1b-inhibitor complex 2qbq Crystal structure of ptp1b-inhibitor complex 2qbr Crystal structure of ptp1b-inhibitor complex 2qbs Crystal structure of ptp1b-inhibitor complex 2qcj Native Structure of Lyp 2qct Structure of Lyp with inhibitor I-C11 2qdc Crystal structure of the HePTP catalytic domain D236A mutant 2qdm Crystal structure of the HePTP catalytic domain C270S/D236A/Q314A mutant 2qdp Crystal structure of the HePTP catalytic domain C270S mutant crystallized in ammonium acetate 2qep Crystal structure of the D1 domain of PTPRN2 (IA2beta) 2shp TYROSINE PHOSPHATASE SHP-2 2veu Crystal structure of protein tyrosine phosphatase 1B in complex with an isothiazolidinone-containing inhibitor 2vev CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR 2vew CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR 2vex CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR 2vey CRYSTAL STRUCUTRE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR 2y2f Crystal structure of Yersinia pestis YopH in complex with an aminooxy- containing platform compound for inhibitor design 2ydu Crystal structure of YopH in complex with 3-(1,1-dioxido-3- oxoisothiazolidin-5-yl)benzaldeyde 2zmm Crystal structure of PTP1B-inhibitor complex 2zn7 CRYSTAL STRUCTURES OF PTP1B-Inhibitor Complexes 3a5j Crystal structure of protein-tyrosine phosphatase 1B 3a5k Crystal structure of protein-tyrosine phosphatase 1B 3b7o Crystal structure of the human tyrosine phosphatase SHP2 (PTPN11) with an accessible active site 3blt Crystal structures of YopH complexed with PVSN and PVS, inhibitors of YopH which co-valent bind to Cys of active site 3blu crystal structure YopH complexed with inhibitor PVS 3bm8 crystal structure of YopH mutant D356A complexed with irreversible inhibitor PVSN 3brh Protein Tyrosine Phosphatase PTPN-22 (Lyp) bound to the mono-Phosphorylated Lck active site peptide 3cwe PTP1B in complex with a phosphonic acid inhibitor 3d42 Crystal structure of HePTP in complex with a monophosphorylated Erk2 peptide 3d44 Crystal structure of HePTP in complex with a dually phosphorylated Erk2 peptide mimetic 3d9c Crystal Structure PTP1B complex with aryl Seleninic acid 3eax Crystal structure PTP1B complex with small molecule compound LZP-6 3eb1 Crystal structure PTP1B complex with small molecule inhibitor LZP-25 3eu0 Crystal structure of the S-nitrosylated Cys215 of PTP1B 3f99 W354F Yersinia enterocolitica PTPase apo form 3f9a W354F Yersinia enterocolitica PTPase complexed with tungstate 3f9b W354F Yersinia enterocolitica PTPase complexed with divanadate 3h2x Crystal Structure of The Human Lymphoid Tyrosine Phosphatase Catalytic Domain 3i36 Crystal Structure of Rat Protein Tyrosine Phosphatase eta Catalytic Domain 3i7z Protein Tyrosine Phosphatase 1B - Transition state analog for the first catalytic step 3i80 Protein Tyrosine Phosphatase 1B - Transition state analog for the second catalytic step 3m4u Crystal Structure of Trypanosoma brucei Protein Tyrosine Phosphatase TbPTP1 3mow Crystal structure of SHP2 in complex with a tautomycetin analog TTN D-1 3o4s Crystal Structure of HePTP with a Closed WPD Loop and an Ordered E-Loop 3o4t Crystal Structure of HePTP with an Open WPD Loop and Partially Depleted Active Site 3o4u Crystal Structure of HePTP with an Atypically Open WPD Loop 3o5x Crystal structure of the oncogenic tyrosine phosphatase SHP2 complexed with a salicylic acid-based small molecule inhibitor 3olr PTPN22 in complex with consensus phospho-tyrosine peptide 1 3omh Crystal structure of PTPN22 in complex with SKAP-HOM pTyr75 peptide 3ps5 Crystal structure of the full-length Human Protein Tyrosine Phosphatase SHP-1 3qcb Human receptor protein tyrosine phosphatase gamma, domain 1, apo 3qcc Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, orthorhombic crystal form 3qcd Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, trigonal crystal form 3qce Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 3-[(3,4-dichlorobenzyl)sulfanyl]thiophene-2-carboxylic acid via soaking 3qcf Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 3-[(3,4-dichlorobenzyl)sulfanyl]thiophene-2-carboxylic acid via co-crystallization 3qcg Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 3-[(3-bromo-4-chlorobenzyl)sulfanyl]thiophene-2-carboxylic acid 3qch Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 3-[(3,4-dichlorobenzyl)sulfanyl]-N-(methylsulfonyl)thiophene-2-carboxamide 3qci Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with N-[(3-aminophenyl)sulfonyl]-3-[(3,4-dichlorobenzyl)sulfanyl]thiophene-2-carboxamide 3qcj Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 5-[({3-[(3,4-dichlorobenzyl)sulfanyl]thiophen-2-yl}carbonyl)sulfamoyl]-2-methoxybenzoic acid 3qck Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 2-[(3,4-dichlorobenzyl)sulfanyl]benzoic acid 3qcl Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 2-[(3,4-dichlorobenzyl)sulfanyl]-4-(4-hydroxybut-1-yn-1-yl)benzoic acid 3qcm Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 2-[(3,4-dichlorobenzyl)sulfanyl]-4-{[3-({N-[2-(methylamino)ethyl]glycyl}amino)phenyl]ethynyl}benzoic acid 3qcn Human receptor protein tyrosine phosphatase gamma, domain 1, trigonal crystal form 3qkp Protein Tyrosine Phosphatase 1B - Apo W179F mutant with open WPD-loop 3qkq Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate 3s3e Crystal structure of the catalytic domain of PTP10D from Drosophila melanogaster 3s3f Crystal Structure of the catalytic domain of PTP10D from Drosophila melanogaster with a small molecule inhibitor Vanadate 3s3h Crystal structure of the catalytic domain of PTP10D from Drosophila melanogaster with a phosphopeptide substrate GP4 3s3k Crystal structure of the catalytic domain of PTP10D from Drosophila melanogaster with a small molecular inhibitor para-NitroCatechol Sulphate 3sme Structure of PTP1B inactivated by H2O2/bicarbonate 3sr9 Crystal structure of mouse PTPsigma 3u96 Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS 3zm0 Catalytic domain of human SHP2 3zm1 Catalytic domain of human SHP2 3zm2 Catalytic domain of human SHP2 3zm3 Catalytic domain of human SHP2 3zmp Src-derived peptide inhibitor complex of PTP1B 3zmq Src-derived mutant peptide inhibitor complex of PTP1B 3zv2 Human protein-tyrosine phosphatase 1b C215A, S216A mutant 4az1 Crystal structure of the Trypanosoma cruzi protein tyrosine phosphatase TcPTP1, a potential therapeutic target for Chagas' disease 4bjo Nitrate in the active site of PTP1b is a putative mimetic of the transition state 4bpc Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form 4dgp The wild-type Src homology 2 (SH2)-domain containing protein tyrosine phosphatase-2 (SHP2) 4dgx LEOPARD Syndrome-Associated SHP2/Y279C mutant 4ge2 Crystal structure of human protein tyrosine phosphatase PTPN9 (MEG2) complex with compound 3 4ge5 Crystal structure of human protein tyrosine phosphatase PTPN9 (MEG2) complex with compound 5 4ge6 Crystal structure of human protein tyrosine phosphatase PTPN9 (MEG2) complex with compound 7 4gfu PTPN18 in complex with HER2-pY1248 phosphor-peptides 4gfv PTPN18 in complex with HER2-pY1196 phosphor-peptides 4gry Crystal structure of SHP1 catalytic domain with SO4 4grz Crystal structure of SHP1 catalytic domain with PO4 4gs0 Crystal structure of SHP1 catalytic domain with JAK1 activation loop peptide 4gwf Crystal structure of the tyrosine phosphatase SHP-2 with Y279C mutation 4h1o Crystal structure of the tyrosine phosphatase SHP-2 with D61G mutation 4h34 Crystal structure of the tyrosine phosphatase SHP-2 with Q506P mutation 4hjp SHP-1 catalytic domain WPD loop open 4hjq SHP-1 catalytic domain WPD loop closed 4i8n CRYSTAL STRUCTURE of PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN INHIBITOR [(4-{(2S)-2-(1,3-BENZOXAZOL-2-YL)-2-[(4-FLUOROPHENYL)SULFAMOYL]ETHYL}PHENYL)AMINO](OXO)ACETIC ACID 4icz HER2 1221/1222 phosphorylation regulated by PTPN9 4ikc Crystal Structure of catalytic domain of PTPRQ 4j51 Cyrstal structure of protein tyrosine phosphatase Lyp catalytic domain complex with small molecular inhibitor L75N04 4nnd 4NND 4nwf 4NWF 4nwg 4NWG 4ohd 4OHD 4ohe 4OHE 4ohh 4OHH 4ohi 4OHI 4ohl 4OHL 4pvg 4PVG 4qah 4QAH 4qap 4QAP 4qbe 4QBE 4qbw 4QBW 4qum 4QUM 4qun 4QUN 4rdd 4RDD 4rh5 4RH5 4rh9 4RH9 4rhg 4RHG 4ri4 4RI4 4ri5 4RI5 4s0g 4S0G 4y14 4Y14 4yaa 4YAA 4z6b 4Z6B 4zi4 4ZI4 4zn5 4ZN5 4zrt 4ZRT 5awx 5AWX 5ehp 5EHP 5ehr 5EHR 5i6v 5I6V 5ibm 5IBM 5ibs 5IBS 5j8r 5J8R - Links (links to other resources describing this domain)
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INTERPRO IPR000242 PFAM Y_phosphatase PROSITE TYR_PHOSPHATASE_PTP