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7AH3

Kinase domain of cSrc in complex with a pyrazolopyrimidine

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 Residues12
Detailsbinding site for residue RCK A 601
ChainResidue
AALA293
AGLY344
ALEU393
AASP404
ALYS295
AVAL323
AILE336
ATHR338
AGLU339
ATYR340
AMET341
ASER342

site_idAC2
Number of Residues1
Detailsbinding site for residue EDO A 602
ChainResidue
AHOH701

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 603
ChainResidue
APRO484
APRO485
AGLU486
ACYS487

site_idAC4
Number of Residues5
Detailsbinding site for residue DMS A 604
ChainResidue
ALYS351
AHOH720
BTYR511
BALA514
BPHE515

site_idAC5
Number of Residues12
Detailsbinding site for residue RCK B 1001
ChainResidue
BVAL281
BALA293
BLYS295
BMET314
BILE336
BTHR338
BGLU339
BMET341
BSER342
BGLY344
BLEU393
BASP404

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO B 1002
ChainResidue
BGLN497
BARG500
BHOH1180

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO B 1003
ChainResidue
AGLY465
AHOH764
BGLU517
BASP518
BHOH1144
BHOH1163

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL B 1004
ChainResidue
AGLU517
AASP518
BLYS427
BPRO464
BGLY465
BHOH1141

site_idAC9
Number of Residues2
Detailsbinding site for residue GOL B 1005
ChainResidue
BGLN362
BARG438

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

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

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
AASP386
BASP386

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU273
BLEU273

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS295
BLYS295

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR416
BTYR416

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR436
BTYR436

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721
ChainResidueDetails
ACYS498
BCYS498

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005
ChainResidueDetails
ATYR527
BTYR527

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PDB entries from 2024-07-17

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