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2C0I

Src family kinase Hck with bound inhibitor A-420983

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A1507
ChainResidue
AGLU498
APTR501
AHOH2166
AHOH2169
AHOH2171
BGLU464

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B1507
ChainResidue
BHOH2088
BHOH2089
BHOH2096
AGLU464
BGLU498
BPTR501

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE L1G A1506
ChainResidue
ALEU247
AALA267
ALYS269
APHE281
AILE310
ATHR312
AGLU313
AMET315
AASP322
ALEU367
AASP378
APHE379
AHOH2173
AHOH2174

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE L1G B1506
ChainResidue
BVAL255
BALA267
BVAL268
BLYS269
BVAL297
BILE310
BTHR312
BGLU313
BMET315
BASP322
BLEU367
BALA377
BASP378
BPHE379
BLEU381
BHOH2099

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGQFGEVWmAtynkhtk...........VAVK
ChainResidueDetails
ALEU247-LYS269

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLRAANILV
ChainResidueDetails
ATYR356-VAL368

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALEU361
BLEU361

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLY248
ATHR270
BGLY248
BTHR270

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ALEU182
BLEU182

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P08103
ChainResidueDetails
AILE189
BILE189

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602
ChainResidueDetails
ATHR391
BTHR391

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AASN442
BASN442

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
AGLU502
BGLU502

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA364
AASP360

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA364
BASP360

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG362
AASP360

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG362
BASP360

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG362
AASP360
AASN365

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG362
BASP360
BASN365

222624

PDB entries from 2024-07-17

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