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2QLQ

Crystal structure of SRC kinase domain with covalent inhibitor RL3

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 SR2 A 1345
ChainResidue
AHOH41
AASP348
ALEU393
AASP404
AALA293
ALYS295
AMET314
AILE336
ATHR338
AGLU339
AMET341
ACYS345

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SR2 A 1483
ChainResidue
ACYS483
APRO484
APRO485
AGLU486
ACYS487
AGLU489

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SR2 B 1345
ChainResidue
BALA293
BLYS295
BILE336
BTHR338
BMET341
BGLY344
BCYS345
BASP348
BALA390
BLEU393
BASP404

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

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

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PDB entries from 2024-07-24

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