The domain within your query sequence starts at position 136 and ends at position 406; the E-value for the STYKc domain shown below is 3.4e-39.

LNYIQEIGSGWFGKVLLGETYTGTSVARVIVKELKVSASPKEQDTFLKSGEPYYILQHPN
VLQCVGQCVEAIPYLLVFEFCDLGDLKAYLHNEQEHVRGDSQTMLLQRMACEIAAGLAAM
HKLHFLHSDLALRNCYLTSDLNVKVGDYGIGFSRYKEDYIETDDKKVFPLRWTAPELVTS
FQDRLLTADQTKYSNIWSLGVTLWELFNNAAQPYANLSDLDVLNQVIRERDMKLPKPQLE
QPYSDRWYEVLQFCWLPPDKRPAAEDVHRLL

STYKc

Protein kinase; unclassified specificity.

• SMART accession number: SM00221
• Description: Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.

There are 7538 STYKc domains in 4685 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Engh RA, Girod A, Kinzel V, Huber R, Bossemeyer D
• Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity.
• J Biol Chem. 1996; 271: 26157-64

The discovery of several hundred different protein kinases involved in highly diverse cellular signaling pathways is in stark contrast to the much smaller number of known modulators of cell signaling. Of these, the H series protein kinase inhibitors (1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H7), N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide (H8) N-[2-(p-Bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H89)) are frequently used to block signaling pathways in studies of cellular regulation. To elucidate inhibition mechanisms at atomic resolution and to enable structure-based drug design of potential therapeutic modulators of signaling pathways, we determined the crystal structures of corresponding complexes with the cAPK catalytic subunit. Complexes with H7 and H8 (2.2 A) and with H89 (2.3 A) define the binding mode of the isoquinoline-sulfonamide derivatives in the ATP-binding site while demonstrating effects of ligand-induced structural change. Specific interactions between the enzyme and the inhibitors include the isoquinoline ring nitrogen ligating to backbone amide of Val-123 and an inhibitor side chain amide bonding to the backbone carbonyl of Glu-170. The conservation of the ATP-binding site of protein kinases allows evaluation of factors governing general selectivity of these inhibitors among kinases. These results should assist efforts in the design of protein kinase inhibitors with specific properties.

• Mohammadi M, Schlessinger J, Hubbard SR
• Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism.
• Cell. 1996; 86: 577-87

The crystal structure of the tyrosine kinase domain of fibroblast growth factor receptor 1 (FGFR1K) has been determined in its unliganded form to 2.0 angstroms resolution and in complex with with an ATP analog to 2.3 angstrosms A resolution. Several features distinguish the structure of FGFR1K from that of the tyrosine kinase domain of the insulin receptor. Residues in the activation loop of FGFR1K appear to interfere with substrate peptide binding but not with ATP binding, revealing a second and perhaps more general autoinhibitory mechanism for receptor tyrosine kinases. In addition, a dimeric form of FGFR1K observed in the crystal structure may provide insights into the molecular mechanisms by which FGF receptors are activated. Finally, the structure provides a basis for rationalizing the effects of kinase mutations in FGF receptors that lead to developmental disorders in nematodes and humans.

• Hanks SK, Hunter T
• Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.
• FASEB J. 1995; 9: 576-96

The eukaryotic protein kinases make up a large superfamily of homologous proteins. They are related by virtue of their kinase domains (also known as catalytic domains), which consist of approximately 250-300 amino acid residues. The kinase domains that define this group of enzymes contain 12 conserved subdomains that fold into a common catalytic core structure, as revealed by the 3-dimensional structures of several protein-serine kinases. There are two main subdivisions within the superfamily: the protein-serine/threonine kinases and the protein-tyrosine kinases. A classification scheme can be founded on a kinase domain phylogeny, which reveals families of enzymes that have related substrate specificities and modes of regulation.

• Owen DJ, Noble ME, Garman EF, Papageorgiou AC, Johnson LN
• Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.
• Structure. 1995; 3: 467-82

BACKGROUND: Control of intracellular events by protein phosphorylation is promoted by specific protein kinases. All the known protein kinase possess a common structure that defines a catalytically competent entity termed the 'kinase catalytic core'. Within this common structural framework each kinase displays its own unique substrate specificity, and a regulatory mechanism that may be modulated by association with other proteins. Structural studies of phosphorylase kinase (Phk), the major substrate of which is glycogen phosphorylase, may be expected to shed light on its regulation. RESULTS: We report two crystal structures of the catalytic core (residues 1-298; Phk gamma trnc) of the gamma-subunit of rabbit muscle phosphorylase kinase: the binary complex with Mn2+/beta-gamma-imidoadenosine 5'-triphosphate (AMPPNP) to a resolution of 2.6 A and the binary complex with Mg2+/ADP to a resolution of 3.0 A. The structures were solved by molecular replacement using the cAMP-dependent protein kinase (cAPK) as a model. CONCLUSIONS: The overall structure of Phk gamma trnc is similar to that of the catalytic core of other protein kinases. It consists of two domians joined on one edge by a 'hinge', with the catalytic site located in the cleft between the domains. Phk gamma trnc is constitutively active, and lacks the need for an activatory phosphorylation event that is essential for many kinases. The structure exhibits an essentially 'closed' conformation of the domains which is similar to that of cAPK complexed with substrates. The phosphorylated residue that is located at the domain interface in many protein kinases and that is believed to stabilize an active conformation is substituted by a glutamate in Phk gamma trnc. The glutamate, in a similar manner to the phosphorylated residue in other protein kinases, interacts with an arginine adjacent to the catalytic aspartate but does not participate in interdomain contacts. The interactions between the enzyme and the nucleotide product of its activity, Mg2+/ADP, explain the inhibitory properties of the nucleotides that are observed in kinetic studies.

• Schulze-Gahmen U et al.
• Multiple modes of ligand recognition: crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine.
• Proteins. 1995; 22: 378-91

Cyclin-dependent kinases (CDKs) are conserved regulators of the eukaryotic cell cycle with different isoforms controlling specific phases of the cell cycle. Mitogenic or growth inhibitory signals are mediated, respectively, by activation or inhibition of CDKs which phosphorylate proteins associated with the cell cycle. The central role of CDKs in cell cycle regulation makes them a potential new target for inhibitory molecules with anti-proliferative and/or anti-neoplastic effects. We describe the crystal structures of the complexes of CDK2 with a weakly specific CDK inhibitor, N6-(delta 2-isopentenyl)adenine, and a strongly specific inhibitor, olomoucine. Both inhibitors are adenine derivatives and bind in the adenine binding pocket of CDK2, but in an unexpected and different orientation from the adenine of the authentic ligand ATP. The N6-benzyl substituent in olomoucine binds outside the conserved binding pocket and is most likely responsible for its specificity. The structural information from the CDK2-olomoucine complex will be useful in directing the search for the next generation inhibitors with improved properties.

• Zhang J, Zhang F, Ebert D, Cobb MH, Goldsmith EJ
• Activity of the MAP kinase ERK2 is controlled by a flexible surface loop.
• Structure. 1995; 3: 299-307

BACKGROUND: The mitogen-activated protein (MAP) kinase, ERK2, is a tightly regulated enzyme in the ubiquitous Ras-activated protein kinase cascade. ERK2 is activated by phosphorylation at two sites, Y185 and T183, that lie in the phosphorylation lip at the mouth of the catalytic site. To ascertain the role of these two residues in securing the low-activity conformation of the enzymes we have carried out crystallographic analyses and assays of phosphorylation-site mutants of ERK2. RESULTS: The crystal structures of four mutants, T183E (threonine at residue 183 is replaced by glutamate), Y185E, Y185F and the double mutant T183E/Y185E, were determined. When T183 is replaced by glutamate, few conformational changes are observed. By contrast, when Y185 is replaced by glutamate, 19 residues become disordered, including the entire phosphorylation lip and an adjacent loop. The conservative substitution of phenylalanine for Y185 also induces relatively large conformational changes. A binding site for phosphotyrosine in the active enzyme is putatively identified on the basis of the high-resolution refinement of the structure of wild-type ERK2. CONCLUSIONS: The remarkable disorder observed throughout the phosphorylation lip when Y185 is mutated shows that the stability of the phosphorylation lip is rather low. Therefore, only modest amounts of binding energy will be required to dislodge the lip for phosphorylation, and it is likely that these residues will be involved in conformational changes associated with both with binding to kinases and phosphatases and with activation. Furthermore, the low-activity structure is specifically dependent on Y185, whereas there is no such dependency on T183. Both residues, however, participate in forming the active enzyme, contributing to its tight control.

• Hubbard SR, Wei L, Ellis L, Hendrickson WA
• Crystal structure of the tyrosine kinase domain of the human insulin receptor.
• Nature. 1994; 372: 746-54

The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 A resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.

• Taylor SS, Radzio-Andzelm E
• Three protein kinase structures define a common motif.
• Structure. 1994; 2: 345-55

Structural comparisons between cAMP-dependent protein kinase, cyclin-dependent kinase 2 and mitogen-activated protein kinase reveal which features are common to the protein kinase family and which are enzyme-specific.

• Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ
• Atomic structure of the MAP kinase ERK2 at 2.3 A resolution.
• Nature. 1994; 367: 704-11

The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

• Bossemeyer D, Engh RA, Kinzel V, Ponstingl H, Huber R
• Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24).
• EMBO J. 1993; 12: 849-59

The crystal structure of the porcine heart catalytic subunit of cAMP-dependent protein kinase in a ternary complex with the MgATP analogue MnAMP-PNP and a pseudosubstrate inhibitor peptide, PKI(5-24), has been solved at 2.0 A resolution from monoclinic crystals of the catalytic subunit isoform CA. The refinement is presently at an R factor of 0.194 and the active site of the molecule is well defined. The glycine-rich phosphate anchor of the nucleotide binding fold motif of the protein kinase is a beta ribbon acting as a flap with conformational flexibility over the triphosphate group. The glycines seem to be conserved to avoid steric clash with ATP. The known synergistic effects of substrate binding can be explained by hydrogen bonds present only in the ternary complex. Implications for the kinetic scheme of binding order are discussed. The structure is assumed to represent a phosphotransfer competent conformation. The invariant conserved residue Asp166 is proposed to be the catalytic base and Lys168 to stabilize the transition state. In some tyrosine kinases Lys168 is functionally replaced by an Arg displaced by two residues in the primary sequence, suggesting invariance in three-dimensional space. The structure supports an in-line transfer with a pentacoordinate transition state at the phosphorus with very few nuclear movements.

• DeBondt HL, Rosenblatt J, Jancarik J, Jones HD, Morgan DO, Kim SH
• Crystal structure of cyclin-dependent kinase 2.
• Nature. 1993; 363: 595-602

Cyclin-dependent kinase 2 (CDK2) is a member of a highly conserved family of protein kinases that regulate the eukaryotic cell cycle. The crystal structures of the human CDK2 apoenzyme and its Mg2+ ATP complex have been determined to 2.4 A resolution. The structure is bi-lobate, like that of the cyclic AMP-dependent protein kinase, but contains a unique helix-loop segment that interferes with ATP and protein substrate binding and probably plays a key part in the regulation of all cyclin-dependent kinases.

• Zheng J et al.
• Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor.
• Biochemistry. 1993; 32: 2154-61

The structure of a ternary complex of the catalytic subunit of cAMP-dependent protein kinase, MgATP, and a 20-residue inhibitor peptide was determined at a resolution of 2.7 A using the difference Fourier technique starting from the model of the binary complex (Knighton et al., 1991a). The model of the ternary complex was refined using both X-PLOR and TNT to an R factor of 0.212 and 0.224, respectively. The orientation of the nucleotide and the interactions of MgATP with numerous conserved residues at the active site of the enzyme are clearly defined. The unique protein kinase nucleotide binding site consists of a five-stranded antiparallel beta-sheet with the base buried in a hydrophobic site along beta-strands 1 and 2 and fixed by hydrogen bonds to the N6 amino and N7 nitrogens. The small lobe secures the nucleotide via a glycine-rich loop and by ion pairing with Lys72 and Glu91. While the small lobe fixes the nontransferable alpha- and beta-phosphates in this inhibitor complex, the gamma-phosphate is secured by two Mg2+ ions and interacts both directly and indirectly with several residues in the large lobe--Asp184, Asn171, Lys168. Asp166 is positioned to serve as a catalytic base. The structure is correlated with previous chemical evidence, and the features that distinguish this nucleotide binding motif from other nucleotide binding proteins are delineated.

• Knighton DR, Zheng JH, TenEyck LF, Xuong NH, Taylor SS, Sowadski JM
• Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
• Science. 1991; 253: 414-20

The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area.

• Knighton DR et al.
• Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
• Science. 1991; 253: 407-14

The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
9.26	map00632	Benzoate degradation via CoA ligation
9.26	map00562	Inositol phosphate metabolism
4.59	map04010	MAPK signaling pathway
3.80	map04060	Cytokine-cytokine receptor interaction
3.80	map04350	TGF-beta signaling pathway
3.24	map04620	Toll-like receptor signaling pathway
3.05	map04730	Long-term depression
3.01	map04540	Gap junction
2.81	map04340	Hedgehog signaling pathway
2.65	map05212	Pancreatic cancer
2.61	map05220	Chronic myeloid leukemia
2.49	map04210	Apoptosis
2.37	map04110	Cell cycle
2.37	map00130	Ubiquinone biosynthesis
2.18	map00230	Purine metabolism
2.14	map04914	Progesterone-mediated oocyte maturation
2.10	map04810	Regulation of actin cytoskeleton
2.10	map05210	Colorectal cancer
1.94	map04520	Adherens junction
1.94	map04111	Cell cycle - yeast
1.82	map04920	Adipocytokine signaling pathway
1.42	map04310	Wnt signaling pathway
1.42	map04910	Insulin signaling pathway
1.42	map05215	Prostate cancer
1.38	map05221	Acute myeloid leukemia
1.27	map04012	ErbB signaling pathway
1.23	map04660	T cell receptor signaling pathway
1.19	map05213	Endometrial cancer
1.19	map04510	Focal adhesion
1.15	map04630	Jak-STAT signaling pathway
1.07	map04360	Axon guidance
1.03	map04140	Regulation of autophagy
1.03	map05214	Glioma
0.99	map05120	Epithelial cell signaling in Helicobacter pylori infection
0.95	map04720	Long-term potentiation
0.95	map04530	Tight junction
0.95	map05219	Bladder cancer
0.95	map05223	Non-small cell lung cancer
0.91	map05211	Renal cell carcinoma
0.91	map05218	Melanoma
0.87	map04150	mTOR signaling pathway
0.87	map04650	Natural killer cell mediated cytotoxicity
0.71	map04912	GnRH signaling pathway
0.67	map04664	Fc epsilon RI signaling pathway
0.59	map05222	Small cell lung cancer
0.55	map04662	B cell receptor signaling pathway
0.47	map04370	VEGF signaling pathway
0.47	map04710	Circadian rhythm
0.44	map04930	Type II diabetes mellitus
0.44	map04916	Melanogenesis
0.32	map04020	Calcium signaling pathway
0.32	map03320	PPAR signaling pathway
0.28	map05216	Thyroid cancer
0.20	map05020	Parkinson's disease
0.12	map00540	Lipopolysaccharide biosynthesis
0.12	map04670	Leukocyte transendothelial migration
0.08	map00350	Tyrosine metabolism
0.08	map04740	Olfactory transduction
0.08	map02020	Two-component system - General
0.08	map00150	Androgen and estrogen metabolism
0.08	map00626	Naphthalene and anthracene degradation
0.08	map04115	p53 signaling pathway
0.08	map00271	Methionine metabolism
0.08	map00361	gamma-Hexachlorocyclohexane degradation
0.08	map00360	Phenylalanine metabolism
0.08	map00380	Tryptophan metabolism
0.08	map00643	Styrene degradation
0.08	map00622	Toluene and xylene degradation
0.08	map00627	1,4-Dichlorobenzene degradation
0.08	map00340	Histidine metabolism
0.08	map00120	Bile acid biosynthesis
0.08	map00363	Bisphenol A degradation
0.08	map00680	Methane metabolism
0.08	map00903	Limonene and pinene degradation
0.08	map00624	1- and 2-Methylnaphthalene degradation
0.04	map05217	Basal cell carcinoma
0.04	map04070	Phosphatidylinositol signaling system
0.04	map04320	Dorso-ventral axis formation
0.04	map05050	Dentatorubropallidoluysian atrophy (DRPLA)

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 STYKc domain which could be assigned to a KEGG orthologous group, and not all proteins containing STYKc 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 STYKc domains in PDB

PDB code	Title
1b6c	CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12
1cki	RECOMBINANT CASEIN KINASE I DELTA TRUNCATION MUTANT CONTAINING RESIDUES 1-317
1ckj	CASEIN KINASE I DELTA TRUNCATION MUTANT CONTAINING RESIDUES 1-317 COMPLEX WITH BOUND TUNGSTATE
1csn	BINARY COMPLEX OF CASEIN KINASE-1 WITH MGATP
1eh4	BINARY COMPLEX OF CASEIN KINASE-1 FROM S. POMBE WITH AN ATP COMPETITIVE INHIBITOR, IC261
1ias	CYTOPLASMIC DOMAIN OF UNPHOSPHORYLATED TYPE I TGF-BETA RECEPTOR CRYSTALLIZED WITHOUT FKBP12
1py5	Crystal Structure of TGF-beta receptor I kinase with inhibitor
1rw8	Crystal Structure of TGF-beta receptor I kinase with ATP site inhibitor
1uwh	The complex of wild type B-RAF and BAY439006
1uwj	The complex of mutant V599E B-RAF and BAY439006
1vjy	Crystal Structure of a Naphthyridine Inhibitor of Human TGF-beta Type I Receptor
1wak	X-ray structure of SRPK1
1wbp	SRPK1 bound to 9mer docking motif peptide
1x8b	Structure of human Wee1A kinase: kinase domain complexed with inhibitor PD0407824
2a19	PKR kinase domain- eIF2alpha- AMP-PNP complex.
2a1a	PKR kinase domain-eIF2alpha Complex
2buj	Crystal structure of the human Serine-threonine Kinase 16 in complex with staurosporine
2c47	Structure of casein kinase 1 gamma 2
2chl	Structure of casein kinase 1 gamma 3
2cmw	Structure of Human Casein kinase 1 gamma-1 in complex with 2-(2- Hydroxyethylamino)-6-(3-chloroanilino)-9-isopropylpurine (CASP TARGET)
2csn	BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7
2eva	Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1
2fb8	Structure of the B-Raf kinase domain bound to SB-590885
2h34	Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE
2in6	Wee1 kinase complex with inhibitor PD311839
2io6	Wee1 kinase complexed with inhibitor PD330961
2izr	Structure of casein kinase gamma 3 in complex with inhibitor
2izs	Structure of casein kinase gamma 3 in complex with inhibitor
2izt	Structure of casein kinase gamma 3 in complex with inhibitor
2izu	Structure of casein kinase gamma 3 in complex with inhibitor
2jii	Structure of vaccinia related kinase 3
2kty	Solution Structure of human Vaccinia Related Kinase-1
2kul	Solution structure of human vaccinia related kinase 1(VRK1)
2lav	NMR solution structure of human Vaccinia-Related Kinase 1
2nru	Crystal structure of IRAK-4
2nry	Crystal structure of IRAK-4
2o8y	Apo IRAK4 Kinase Domain
2oib	Crystal structure of IRAK4 kinase domain apo form
2oic	Crystal structure of IRAK4 kinase domain complexed with staurosporine
2oid	Crystal structure of IRAK4 kinase domain complexed with AMPPNP
2pml	Crystal structure of PfPK7 in complex with an ATP analogue
2pmn	Crystal structure of PfPK7 in complex with an ATP-site inhibitor
2pmo	Crystal structure of PfPK7 in complex with hymenialdisine
2pzi	Crystal Structure of Protein kinase PknG from Mycobacterium tuberculosis in Complex with Tetrahydrobenzothiophene AX20017
2qkw	Structural basis for activation of plant immunity by bacterial effector protein AvrPto
2qlu	Crystal structure of Activin receptor type II kinase domain from human
2rio	Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing
2rsv	Solution structure of human full-length vaccinia related kinase 1 (VRK1)
2v62	Structure of vaccinia-related kinase 2
2vuw	Structure of human haspin kinase domain
2vwb	Structure of the archaeal Kae1-Bud32 fusion protein MJ1130: a model for the eukaryotic EKC-KEOPS subcomplex involved in transcription and telomere homeostasis.
2w1z	ROP2 from Toxoplasma gondii: A virulence factor with a protein- kinase fold and no enzymatic activity.
2wb8	Crystal structure of Haspin kinase
2wot	ALK5 IN COMPLEX WITH 4-((5,6-dimethyl-2-(2-pyridyl)-3-pyridyl)oxy)-N-( 3,4,5-trimethoxyphenyl)pyridin-2-amine
2wou	ALK5 IN COMPLEX WITH 4-((4-((2,6-dimethyl-3-pyridyl)oxy)-2-pyridyl) amino)benzenesulfonamide
2wtk	Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex
2x7g	Structure of human serine-arginine-rich protein-specific kinase 2 ( SRPK2) bound to purvalanol B
2x7o	Crystal structure of TGFbRI complexed with an indolinone inhibitor
2y4i	KSR2-MEK1 heterodimer
2yiy	Crystal structure of compound 8 bound to TAK1-TAB
2z2w	Humand Wee1 kinase complexed with inhibitor PF0335770
3beg	Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2
3bi6	Wee1 kinase complex with inhibitor PD352396
3biz	Wee1 kinase complex with inhibitor PD331618
3byv	Crystal structure of Toxoplasma gondii specific rhoptry antigen kinase domain
3c4c	B-Raf Kinase in Complex with PLX4720
3cqe	Wee1 kinase complex with inhibitor PD074291
3cr0	Wee1 kinase complex with inhibitor PD259_809
3d4q	Pyrazole-based inhibitors of B-Raf kinase
3dlz	Crystal structure of human haspin in complex with AMP
3dzo	Crystal structure of a rhoptry kinase from toxoplasma gondii
3e7v	Crystal Structure of Human Haspin with a pyrazolo-pyrimidine ligand
3en9	Structure of the Methanococcus jannaschii KAE1-BUD32 fusion protein
3enh	Crystal structure of Cgi121/Bud32/Kae1 complex
3f2n	Crystal Structure of Human Haspin with an Imidazo-pyridazine ligand
3faa	Crystal structure of TGFbRI complexed with a 2-aminoimidazole inhibitor
3fbv	Crystal structure of the oligomer formed by the kinase-ribonuclease domain of Ire1
3fmd	Crystal Structure of Human Haspin with an Isoquinoline ligand
3fpq	Crystal structure of the kinase domain of WNK1
3g2f	Crystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution
3gni	Structure of STRAD and MO25
3gxl	ALK-5 kinase complex with GW857175
3h9r	Crystal structure of the kinase domain of type I activin receptor (ACVR1) in complex with FKBP12 and dorsomorphin
3hgk	crystal structure of effect protein AvrptoB complexed with kinase Pto
3hmm	Structure of Alk5 + GW855857
3idp	B-Raf V600E kinase domain in complex with an aminoisoquinoline inhibitor
3ii5	The Complex of wild-type B-RAF with Pyrazolo pyrimidine inhibitor
3iq7	Crystal Structure of human Haspin in complex with 5-Iodotubercidin
3kcf	Crystal structure of TGFbRI complexed with a pyrazolone inhibitor
3kmu	Crystal structure of the ILK/alpha-parvin core complex (apo)
3kmw	Crystal structure of the ILK/alpha-parvin core complex (MgATP)
3lj0	IRE1 complexed with ADP and Quercetin
3lj1	IRE1 complexed with Cdk1/2 Inhibitor III
3lj2	IRE1 complexed with JAK Inhibitor I
3mdy	Crystal structure of the cytoplasmic domain of the bone morphogenetic protein receptor type-1B (BMPR1B) in complex with FKBP12 and LDN-193189
3mtf	Crystal structure of the ACVR1 kinase in complex with a 2-aminopyridine inhibitor
3my0	Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189
3og7	B-Raf Kinase V600E oncogenic mutant in complex with PLX4032
3omv	Crystal structure of c-raf (raf-1)
3oom	Crystal structure of the ACVR1 kinase domain in complex with the imidazo[1,2-b]pyridazine inhibitor K00507
3op5	Human vaccinia-related kinase 1
3orm	Mycobacterium tuberculosis PknB kinase domain D76A mutant
3p1a	Structure of human Membrane-associated Tyrosine- and Threonine-specific cdc2-inhibitory kinase MYT1 (PKMYT1)
3p23	Crystal structure of the Human kinase and RNase domains in complex with ADP
3p86	Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine
3ppj	Human B-Raf Kinase in Complex with a Furopyridine Inhibitor
3ppk	Human B-Raf Kinase in Complex with a Non-Oxime Furopyridine Inhibitor
3prf	Crystal Structure of Human B-Raf Kinase Domain in Complex with a Non-Oxime Furopyridine Inhibitor
3pri	Crystal Structure of Human B-Raf Kinase in Complex with a Non-Oxime Furopyridine Inhibitor
3psb	Furo[2,3-c]pyridine-based Indanone Oximes as Potent and Selective B-Raf Inhibitors
3psd	Non-oxime pyrazole based inhibitors of B-Raf kinase
3q4c	Crystal Structure of Wild Type BRAF kinase domain in complex with organometallic inhibitor CNS292
3q4t	Crystal structure of Activin receptor type-IIA (ACVR2A) kinase domain in complex with dorsomorphin
3q4u	Crystal structure of the ACVR1 kinase domain in complex with LDN-193189
3q5z	Crystal structure of virulent allele ROP5B pseudokinase domain
3q60	Crystal structure of virulent allele ROP5B pseudokinase domain bound to ATP
3q96	B-Raf kinase domain in complex with a tetrahydronaphthalene inhibitor
3qa8	Crystal Structure of inhibitor of kappa B kinase beta
3qd2	Crsytal structure of mouse PERK kinase domain
3rep	Crystal structure of the ILK/alpha-parvin core complex (MnATP)
3rzf	Crystal Structure of Inhibitor of kappaB kinase beta (I4122)
3s95	Crystal structure of the human LIMK1 kinase domain in complex with staurosporine
3sdj	Structure of RNase-inactive point mutant of oligomeric kinase/RNase Ire1
3sdm	Structure of oligomeric kinase/RNase Ire1 in complex with an oligonucleotide
3skc	Human B-Raf Kinase in Complex with an Amide Linked Pyrazolopyridine Inhibitor
3soc	Crystal structure of Activin receptor type-IIA (ACVR2A) kinase domain in complex with a quinazolin
3sv0	Crystal structure of casein kinase-1 like protein in plant
3tl8	The AvrPtoB-BAK1 complex reveals two structurally similar kinaseinteracting domains in a single type III effector
3tv4	Human B-Raf Kinase Domain in Complex with an Bromopyridine Benzamide Inhibitor
3tv6	Human B-Raf Kinase Domain in Complex with a Methoxypyrazolopyridinyl Benzamide Inhibitor
3tzm	TGF-beta Receptor type 1 in complex with SB431542
3uim	Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation
3uiu	Crystal structure of Apo-PKR kinase domain
3ulz	Crystal structure of apo BAK1
3uys	Crystal structure of apo human ck1d
3uyt	crystal structure of ck1d with PF670462 from P1 crystal form
3uzp	crystal structure of ck1d with PF670462 from P21 crystal form
3zon	Human TYK2 pseudokinase domain bound to a kinase inhibitor
4asx	Crystal structure of Activin receptor type-IIA (ACVR2A) kinase domain in complex with a beta-carboline inhibitor
4ax8	Medium resolution structure of the bifunctional kinase- methyltransferase WbdD
4azs	High resolution (2.2 A) crystal structure of WbdD.
4azt	Co-crystal structure of WbdD and kinase inhibitor LY294002.
4azv	Co-crystal structure of WbdD and kinase inhibitor GW435821x.
4azw	Crystal structure of monomeric WbdD.
4bgg	Crystal structure of the ACVR1 kinase in complex with LDN-213844
4btf	Structure of MLKL
4btj	TTBK1 in complex with ATP
4btk	TTBK1 in complex with inhibitor
4btm	TTBK1 in complex with inhibitor
4bwk	Structure of Neurospora crassa PAN3 pseudokinase
4bwp	Structure of Drosophila Melanogaster PAN3 pseudokinase
4bwx	Structure of Neurospora crassa PAN3 pseudokinase mutant
4c02	Crystal structure of human ACVR1 (ALK2) in complex with FKBP12.6 and dorsomorphin
4c57	Structure of GAK kinase in complex with a nanobody
4c58	Structure of GAK kinase in complex with nanobody (NbGAK_4)
4c59	Structure of GAK kinase in complex with nanobody (NbGAK_4)
4c8b	Structure of the kinase domain of human RIPK2 in complex with ponatinib
4ci6	4CI6
4cqe	4CQE
4cyi	4CYI
4cyj	4CYJ
4czy	4CZY
4dbn	Crystal Structure of the Kinase domain of Human B-raf with a [1,3]thiazolo[5,4-b]pyridine derivative
4dn5	Crystal Structure of NF-kB-inducing Kinase (NIK)
4dym	Crystal structure of the ACVR1 kinase domain in complex with the imidazo[1,2-b]pyridazine inhibitor K00135
4e26	BRAF in complex with an organic inhibitor 7898734
4e3c	X-ray crystal structure of human IKK2 in an active conformation
4e4x	Crystal Structure of B-Raf Kinase Domain in Complex with a Dihydropyrido[2,3-d]pyrimidinone-based Inhibitor
4ehe	B-Raf Kinase Domain in Complex with an Aminothienopyrimidine-based Inhibitor
4ehg	B-Raf Kinase Domain in Complex with an Aminopyridimine-based Inhibitor
4eut	Structure of BX-795 Complexed with Unphosphorylated Human TBK1 Kinase-ULD Domain
4euu	Structure of BX-795 Complexed with Human TBK1 Kinase Domain Phosphorylated on Ser172
4f0f	Crystal Structure of the Roco4 Kinase Domain bound to AppCp from D. discoideum
4f0g	Crystal Structure of the Roco4 Kinase Domain from D. discoideum
4f1m	Crystal Structure of the G1179S Roco4 Kinase Domain bound to AppCp from D. discoideum.
4f1o	Crystal Structure of the L1180T mutant Roco4 Kinase Domain from D. discoideum bound to AppCp
4f1t	Crystal Structure of the Roco4 Kinase Domain from D. discoideum bound to the ROCK Inhibitor H1152
4f99	Human CDC7 kinase in complex with DBF4 and nucleotide
4f9a	Human CDC7 kinase in complex with DBF4 and nucleotide
4f9b	Human CDC7 kinase in complex with DBF4 and PHA767491
4f9c	Human CDC7 kinase in complex with DBF4 and XL413
4fc0	Crystal Structure of Human Kinase Domain of B-raf with a DFG-out Inhibitor
4fi1	Crystal structure of scCK2 alpha in complex with ATP
4fk3	B-Raf Kinase V600E Oncogenic Mutant in Complex with PLX3203
4fvp	Crystal structure of the Jak2 pseudokinase domain (apo form)
4fvq	Crystal structure of the Jak2 pseudokinase domain (Mg-ATP-bound form)
4fvr	Crystal structure of the Jak2 pseudokinase domain mutant V617F (Mg-ATP-bound form)
4g16	Crystal structure of ck1g3 with 2-[(4-{[3-(TRIFLUOROMETHYL)PYRIDIN2-YL]OXY}PHENYL)AMINO]-1H-BENZIMIDAZOLE-6-CARBONITRILE
4g17	Crystal structure of ck1g3 with 2-[(4-TERT-BUTYLPHENYL)AMINO]-1H-BENZIMIDAZOLE-6-CARBONITRILE
4g31	Crystal Structure of GSK6414 Bound to PERK (R587-R1092, delete A660-T867) at 2.28 A Resolution
4g34	Crystal Structure of GSK6924 Bound to PERK (R587-R1092, delete A660-T867) at 2.70 A Resolution
4g3c	Crystal structure of apo murine Nf-kappaB inducing kinase (NIK)
4g3d	Crystal structure of human NF-kappaB inducing kinase (NIK)
4g3e	Crystal structure of murine NF-kappaB inducing kinase (NIK) bound to a 6-alkynylindoline (cmp1)
4g3f	Crystal structure of murine NF-kappaB inducing kinase (NIK) bound to a 2-(aminothiazoly)phenol (cmp2)
4g3g	Crystal structure of murine NF-kappaB inducing kinase (NIK) V408L bound to a 2-(aminothiazolyl)phenol (cmp3)
4g9c	Human B-Raf Kinase Domain bound to a Type II Pyrazolopyridine Inhibitor
4g9r	B-Raf V600E Kinase Domain Bound to a Type II Dihydroquinazoline Inhibitor
4gs6	Irreversible Inhibition of TAK1 Kinase by 5Z-7-Oxozeaenol
4h58	BRAF in complex with compound 3
4hgl	Crystal structure of ck1g3 with compound 1
4hgs	Crystal structure of ck1gs with compound 13
4hgt	Crystal structure of ck1d with compound 13
4hnf	Crystal structure of ck1d in complex with pf4800567
4hni	crystal structure of ck1e in complex with PF4800567
4hok	crystal structure of apo ck1e
4i92	Structure of the BSK8 kinase domain
4i93	Structure of the BSK8 kinase domain (SeMet labeled)
4i94	Structure of BSK8 in complex with AMP-PNP
4idt	Crystal Structure of NIK with 11-bromo-5,6,7,8-tetrahydropyrimido[4',5':3,4]cyclohepta[1,2-b]indol-2-amine (T28)
4idv	Crystal Structure of NIK with compound 4-{3-[2-amino-5-(2-methoxyethoxy)pyrimidin-4-yl]-1H-indol-5-yl}-2-methylbut-3-yn-2-ol (13V)
4im0	Structure of Tank-Binding Kinase 1
4im2	Structure of Tank-Binding Kinase 1
4im3	Structure of Tank-Binding Kinase 1
4ith	Crystal structure of RIP1 kinase in complex with necrostatin-1 analog
4iti	Crystal structure of RIP1 kinase in complex with necrostatin-3 analog
4itj	Crystal structure of RIP1 kinase in complex with necrostatin-4
4iw0	Crystal structure and mechanism of activation of TBK1
4iwo	Crystal structure and mechanism of activation of TBK1
4iwp	Crystal structure and mechanism of activation of TBK1
4iwq	Crystal structure and mechanism of activation of TBK1
4ix3	Crystal structure of a Stt7 homolog from Micromonas algae
4ix4	Crystal structure of a Stt7 homolog from Micromonas algae in complex with ADP
4ix5	Crystal structure of a Stt7 homolog from Micromonas algae in complex with AMP-PNP
4ix6	Crystal structure of a Stt7 homolog from Micromonas algae soaked with ATP
4jjr	A P21 crystal form of mammalian casein kinase 1 delta
4jl9	Crystal structure of mouse TBK1 bound to BX795
4jlc	Crystal structure of mouse TBK1 bound to SU6668
4jqe	Crystal structure of scCK2 alpha in complex with AMPPN
4jr7	Crystal structure of scCK2 alpha in complex with GMPPNP
4jrn	ROP18 kinase domain in complex with AMP-PNP and sucrose
4jvg	B-Raf Kinase in Complex with Birb796
4kb8	CK1d in complex with 1-{4-[3-(4-FLUOROPHENYL)-1-METHYL-1H-PYRAZOL-4-YL]PYRIDIN-2-YL}-N-METHYLMETHANAMINE ligand
4kba	CK1d in complex with 9-[3-(4-fluorophenyl)-1-methyl-1H-pyrazol-4-yl]-2,3,4,5-tetrahydropyrido[2,3-f][1,4]oxazepine inhibitor
4kbc	CK1d in complex with {4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDIN-2-YL}METHANOL inhibitor
4kbk	CK1d in complex with (3S)-3-{4-[3-(4-fluorophenyl)-1-methyl-1H-pyrazol-4-yl]pyridin-2-yl}morpholine inhibitor
4kik	Human IkB kinase beta
4ksp	Crystal Structure of Human B-raf bound to a DFG-out Inhibitor TAK-632
4ksq	Crystal Structure of Human B-raf bound to a DFG-out Inhibitor 5B
4l00	Crystal structure of the apo Jak1 pseudokinase domain
4l01	Crystal structure of the V658F apo Jak1 pseudokinase domain
4l3p	Crystal Structure of 2-(1-benzothiophen-7-yl)-4-[1-(piperidin-4-yl)-1H-pyrazol-4-yl]furo[2,3-c]pyridin-7-amine bound to TAK1-TAB1
4l52	Crystal Structure of 1-(4-{4-[7-amino-2-(1,2,3-benzothiadiazol-7-yl)furo[2,3-c]pyridin-4-yl]-1H-pyrazol-1-yl}piperidin-1-yl)ethan-1-one bound to TAK1-TAB1
4l53	Crystal Structure of (1R,4R)-4-{4-[7-amino-2-(1,2,3-benzothiadiazol-7-yl)-3-chlorofuro[2,3-c]pyridin-4-yl]-1H-pyrazol-1-yl}cyclohexan-1-ol bound to TAK1-TAB1
4l68	Structure of the psedudokinase domain of BIR2, an immune regulator of the RLK/Pelle family
4lfi	Crystal structure of scCK2 alpha in complex with GMPPNP
4lv5	Murine IRGa6 bound to Toxoplasma ROP5B, a pseudokinase GDI
4lv8	Murine IRGa6 bound to Toxoplasma ROP5C, a pseudokinase GDI
4m66	Crystal structure of the mouse RIP3 kinase domain
4m67	Crystal structure of the human MLKL kinase-like domain
4m68	Crystal structure of the mouse MLKL kinase-like domain
4m69	Crystal structure of the mouse RIP3-MLKL complex
4m7i	4M7I
4mbj	Human B-Raf Kinase Domain in Complex with an Imidazopyridine-based Inhibitor
4mne	4MNE
4mnf	4MNF
4mwh	Crystal structure of scCK2 alpha in complex with ATP
4mwi	Crystal structure of the human MLKL pseudokinase domain
4neu	X-ray structure of Receptor Interacting Protein 1 (RIP1)kinase domain with a 1-aminoisoquinoline inhibitor
4nfm	Human tau tubulin kinase 1 (TTBK1)
4nfn	Human tau tubulin kinase 1 (TTBK1) complexed with 3-({5-[(4-amino-4-methylpiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-bromophenol
4nt4	Crystal structure of the kinase domain of Gilgamesh isoform I from Drosophila melanogaster
4o1o	Crystal Structure of RNase L in complex with 2-5A
4o1p	Crystal Structure of RNase L in complex with 2-5A and AMP-PNP
4o38	Crystal structure of the human cyclin G associated kinase (GAK)
4o91	4O91
4oau	Complete human RNase L in complex with biological activators.
4oav	Complete human RNase L in complex with 2-5A (5'-ppp heptamer), AMPPCP and RNA substrate.
4oh4	4OH4
4oli	4OLI
4ouc	Structure of human haspin in complex with histone H3 substrate
4ow8	4OW8
4pl3	4PL3
4pl4	4PL4
4pl5	4PL5
4pp7	Highly Potent and Selective 3-N-methylquinazoline-4(3H)-one Based Inhibitors of B-RafV600E Kinase
4pwn	4PWN
4q2a	4Q2A
4q5j	4Q5J
4qpm	4QPM
4qtc	4QTC
4r5y	4R5Y
4r8q	4R8Q
4rmz	4RMZ
4rzv	4RZV
4rzw	4RZW
4tn6	4TN6
4tpt	4TPT
4tw9	4TW9
4twc	4TWC
4u6r	4U6R
4u97	4U97
4u9a	4U9A
4uw0	4UW0
4w9w	4W9W
4w9x	4W9X
4wo5	4WO5
4wov	4WOV
4wsq	4WSQ
4wua	4WUA
4ww5	4WW5
4ww7	4WW7
4ww9	4WW9
4wwa	4WWA
4x0m	4X0M
4x2f	4X2F
4x2g	4X2G
4x2j	4X2J
4x2k	4X2K
4x2n	4X2N
4x3f	4X3F
4x7h	4X7H
4x7j	4X7J
4x7k	4X7K
4x7l	4X7L
4x7n	4X7N
4x7o	4X7O
4xh0	4XH0
4xhg	4XHG
4xhh	4XHH
4xhl	4XHL
4xr7	4XR7
4xs2	4XS2
4xv1	4XV1
4xv2	4XV2
4xv3	4XV3
4xv9	4XV9
4y0x	4Y0X
4y12	4Y12
4y73	4Y73
4y83	4Y83
4y85	4Y85
4y8d	4Y8D
4yff	4YFF
4yfi	4YFI
4yht	4YHT
4yo6	4YO6
4yp8	4YP8
4yz9	4YZ9
4yzc	4YZC
4yzd	4YZD
4yzm	4YZM
4yzn	4YZN
4z7g	4Z7G
4z7h	4Z7H
4ztl	4ZTL
4ztm	4ZTM
4ztn	4ZTN
5ar2	5AR2
5ar3	5AR3
5ar4	5AR4
5ar5	5AR5
5ar7	5AR7
5ar8	5AR8
5c01	5C01
5c03	5C03
5c9c	5C9C
5ce3	5CE3
5cek	5CEK
5cem	5CEM
5cen	5CEN
5ceo	5CEO
5cep	5CEP
5ceq	5CEQ
5ckw	5CKW
5clr	5CLR
5csw	5CSW
5csx	5CSX
5ct7	5CT7
5cyz	5CYZ
5czo	5CZO
5dfz	5DFZ
5dmz	5DMZ
5drb	5DRB
5e7r	5E7R
5e8s	5E8S
5e8t	5E8T
5e8u	5E8U
5e8v	5E8V
5e8w	5E8W
5e8x	5E8X
5e8y	5E8Y
5e8z	5E8Z
5e90	5E90
5e91	5E91
5e92	5E92
5ebz	5EBZ
5fd2	5FD2
5fqd	5FQD
5fri	5FRI
5gjd	5GJD
5gjf	5GJF
5gjg	5GJG
5hes	5HES
5hgi	5HGI
5hi2	5HI2
5hid	5HID
5hie	5HIE
5htb	5HTB
5htc	5HTC
5hvj	5HVJ
5hvk	5HVK
5hx6	5HX6
5i3o	5I3O
5i3r	5I3R
5i4n	5I4N
5ih4	5IH4
5ih5	5IH5
5ih6	5IH6
5ikw	5IKW
5ita	5ITA
5iu2	5IU2
5j0a	5J0A
5j79	5J79
5j7b	5J7B
5jga	5JGA
5jgb	5JGB
5jgd	5JGD
5jrq	5JRQ
5jsm	5JSM
5jt2	5JT2
5kc2	5KC2
5khu	5KHU
5kkr	5KKR
5knj	5KNJ
5ko1	5KO1
5kx7	5KX7
5kx8	5KX8
5l4q	5L4Q
5l6w	5L6W
5lpb	5LPB
5lpv	5LPV
5lpw	5LPW
5lpy	5LPY
5lpz	5LPZ
5te0	5TE0
5tf9	5TF9
5tkx	5TKX
5tqw	5TQW
5tqx	5TQX
5tqy	5TQY