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3VS1

Crystal structure of HCK complexed with a pyrrolo-pyrimidine inhibitor 1-[4-(4-amino-7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-5-yl)phenyl]-3-phenylurea

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 Residues4
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AGLU524
APTR527
AGLU529
BGLU490

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 603
ChainResidue
AARG85
AARG123
AARG128

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VSA A 602
ChainResidue
AALA293
ALEU325
AILE336
ATHR338
AGLU339
AMET341
ALEU393
AASP404
ALEU273
AVAL281

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 601
ChainResidue
AGLU490
AHOH750
BGLU524
BPTR527
BGLU529

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 603
ChainResidue
BARG85
BARG123
BARG128

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE VSA B 602
ChainResidue
BVAL281
BALA293
BLYS295
BLEU325
BILE336
BTHR338
BGLU339
BPHE340
BMET341
BSER345
BLEU393
BASP404
BHOH701

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
BLEU273
BLYS295
ALEU273
ALYS295

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

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PDB entries from 2024-05-29

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