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2HCK

SRC FAMILY KINASE HCK-QUERCETIN COMPLEX

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 B 1
ChainResidue
AGLU524
APTR527
AGLN529
BGLU490

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 2
ChainResidue
AGLU490
BGLU524
BPTR527
BGLN529

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE QUE A 1
ChainResidue
AALA293
ATHR338
AGLU339
APHE340
AMET341
AGLY344
ALEU393
ALEU273

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE QUE B 532
ChainResidue
BLEU273
BVAL281
BALA293
BTHR338
BGLU339
BMET341
BGLY344
BASP348
BLEU393
BHOH534

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
ALEU273
ALYS295
BLEU273
BLYS295

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR206
BTHR206

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P08103
ChainResidueDetails
ATYR213
BTYR213

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602
ChainResidueDetails
AILE426
BILE426

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AARG477
BARG477

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

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

237735

PDB entries from 2025-06-18

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