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2HWO

Crystal structure of Src kinase domain in complex with covalent inhibitor

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 Residues8
DetailsBINDING SITE FOR RESIDUE RBS A 1345
ChainResidue
ALEU273
AVAL281
ATHR338
AGLY344
ACYS345
AALA390
ALEU393
AASP404

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RBS B 1345
ChainResidue
BLEU273
BTHR338
BMET341
BGLY344
BCYS345
BALA390
BLEU393
BASP404
BHOH29

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 100
ChainResidue
AARG460
BGLU510
BGLN513

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
ALEU387
BLEU387

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AGLY274
BGLY274

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATHR296
BTHR296

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081
ChainResidueDetails
ATHR417
BTHR417

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081
ChainResidueDetails
AGLY437
BGLY437

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721
ChainResidueDetails
ATRP499
BTRP499

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005
ChainResidueDetails
AGLN528
BGLN528

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP386
AALA390

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP386
BALA390

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG388
AASP386

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG388
BASP386

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG388
AASN391
AASP386

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG388
BASN391
BASP386

226707

PDB entries from 2024-10-30

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