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2SRC

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC, IN COMPLEX WITH AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP A 1
ChainResidue
ALEU273
ASER345
AASP386
AARG388
AASN391
ALEU393
AASP404
AHOH1064
AHOH1147
AHOH1200
AHOH1208
AGLY276
AHOH1230
AVAL281
AALA293
ALYS295
ATHR338
AGLU339
ATYR340
AMET341

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 Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALEU387

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY274
ATHR296

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05480
ChainResidueDetails
ACYS185

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by FAK2 => ECO:0000250
ChainResidueDetails
ATHR417

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:26936507, ECO:0000269|PubMed:7525268, ECO:0000269|PubMed:7929427, ECO:0007744|PubMed:19369195
ChainResidueDetails
AGLN528

218853

PDB entries from 2024-04-24

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