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3VS4

Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 5-(4-phenoxyphenyl)-7-(tetrahydro-2H-pyran-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AGLU490
BGLU524
BPTR527

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 602
ChainResidue
AARG85
AARG123
AARG128

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VSF A 603
ChainResidue
AVAL323
ATHR338
AGLU339
AMET341
ASER345
AASP404
APHE405
AVAL281
AALA293
ALYS295

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 601
ChainResidue
AGLU524
APTR527
BGLU490
BHOH717

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 602
ChainResidue
BARG123
BARG128

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE VSF B 603
ChainResidue
BLEU273
BVAL281
BALA293
BLYS295
BVAL323
BLEU325
BTHR338
BGLU339
BMET341
BLEU393
BASP404
BPHE405
BHOH775

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGQFGEVWmAtynkhtk...........VAVK
ChainResidueDetails
ALEU273-LYS295

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLRAANILV
ChainResidueDetails
ATYR382-VAL394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP386
BASP386

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALEU273
ALYS295
BLEU273
BLYS295

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR207
BTHR207

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P08103
ChainResidueDetails
ATYR214
BTYR214

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602
ChainResidueDetails
ATYR416
BTYR416

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER467
BSER467

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10360180, ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:16216497, ECO:0000269|PubMed:9024658
ChainResidueDetails
APTR527
BPTR527

220113

PDB entries from 2024-05-22

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