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3MJ1

X-ray crystal structure of ITK complexed with inhibitor RO5191614

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 614 A 1
ChainResidue
AHOH45
AHIS440
AGLY441
ACYS442
ALEU489
AHOH137
AILE369
ASER371
AALA389
AGLU436
APHE437
AMET438
AGLU439

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGQFGLVHlGywlnkdk...........VAIK
ChainResidueDetails
AILE369-LYS391

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VIHrDLAARNCLV
ChainResidueDetails
AVAL478-VAL490

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP482

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE369
ALYS391

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by LCK => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR512

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER565

218853

PDB entries from 2024-04-24

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