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3V8W

Crystal Structure of Interleukin-2 Inducible T-cell Kinase Itk Catalytic Domain with Thienopyrazolylindole Inhibitor 469

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
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0G2 A 701
ChainResidue
AILE369
ALEU489
ASER499
AASP500
AALA389
ALYS391
APHE435
AGLU436
APHE437
AMET438
AGLU439
AGLY441

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 701
ChainResidue
AARG451
ALYS556
BARG451
BLYS556

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0G2 B 702
ChainResidue
BILE369
BALA389
BLYS391
BPHE435
BGLU436
BPHE437
BMET438
BGLU439
BHIS440
BGLY441
BLEU489
BSER499

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP482
BASP482

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE369
ALYS391
BILE369
BLYS391

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by LCK => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR512
BTYR512

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER565
BSER565

221716

PDB entries from 2024-06-26

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