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3V8T

Crystal Structure of Interleukin-2 Inducible T-cell Kinase Itk Catalytic Domain with Thienopyrazolylindole Inhibitor 477

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 Residues13
DetailsBINDING SITE FOR RESIDUE 477 A 701
ChainResidue
AILE369
AGLY441
ALEU489
ASER499
B477701
AALA389
ALYS391
APHE435
AGLU436
APHE437
AMET438
AGLU439
AHIS440

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 477 B 701
ChainResidue
A477701
BILE369
BALA389
BLYS391
BPHE435
BGLU436
BPHE437
BMET438
BGLU439
BHIS440
BGLY441
BLEU489
BSER499

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 702
ChainResidue
AARG451
ALYS556
AHOH873
BARG451
BLYS556
BHOH834
BHOH865

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

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PDB entries from 2024-07-24

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