The domain within your query sequence starts at position 867 and ends at position 1127; the E-value for the PTPc domain shown below is 3.37e-133.

All catalytic sites are present in this domain. Check the literature (PubMed 98221181 ) for details.

GFAEEYEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANY
MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ
DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFR
YLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRP
LMVQTEDQYVFLNQCVLDIIR

PTPc

Protein tyrosine phosphatase, catalytic domain

• SMART accession number: SM00194
• 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) ]:

  • (1) pTyr-specific phosphatases
  • (2) dual specificity phosphatases (dTyr and dSer/dThr)
  • (3) Cdc25 phosphatases (dTyr and/or dThr)
  • (4) LMW (low molecular weight) phosphatases

  Based on their cellular localisation, PTPases are also classified as:

  • Receptor-like, which are transmembrane receptors that contain PTPase domains [ (PUBMED:16672235) ]
  • Non-receptor (intracellular) PTPases [ (PUBMED:8948575) ]

  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)

There are 37989 PTPc domains in 29134 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: signalling
Binding / catalysis: protein tyrosine phosphatase

Literature (relevant references for this domain)

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

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

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

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

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

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

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

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

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

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

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

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

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)

% 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	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)

• INTERPRO: IPR000242
• PFAM: Y_phosphatase
• PROSITE: TYR_PHOSPHATASE_PTP