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5AOK

Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan7099

Functional Information from GO Data
ChainGOidnamespacecontents
A0000976molecular_functiontranscription cis-regulatory region binding
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0005634cellular_componentnucleus
A0006355biological_processregulation of DNA-templated transcription
A0006915biological_processapoptotic process
B0000976molecular_functiontranscription cis-regulatory region binding
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0005634cellular_componentnucleus
B0006355biological_processregulation of DNA-templated transcription
B0006915biological_processapoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1291
ChainResidue
APRO219
AGLU221
ATHR230
ATHR231
AILE232
AGOH1292
AHOH2212
AHOH2213

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1313
ChainResidue
AHIS179
ACYS238
ACYS242
ACYS176

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 1292
ChainResidue
BPRO219
BCYS220
BGLU221
BTHR230
BTHR231
BILE232
BGOH1294
BHOH2196
BHOH2197

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 1293
ChainResidue
BHIS115
BSER116
BGLY117
BARG282

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1300
ChainResidue
BCYS176
BHIS179
BCYS238
BCYS242

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOH A 1292
ChainResidue
AVAL147
ATHR150
APRO151
ACYS220
AGLU221
APRO223
ATHR230
AGOL1291
AHOH2094
AHOH2095
AHOH2107
AHOH2288

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GOH B 1294
ChainResidue
BVAL147
BTHR150
BPRO151
BPRO152
BCYS220
BGLU221
BPRO223
BTHR230
BGOL1292
BHOH2082
BHOH2083
BHOH2084
BHOH2097
BHOH2278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues380
DetailsDNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
ChainResidueDetails
ATHR102-LYS292
BTHR102-LYS292

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
ChainResidueDetails
ACYS176
AHIS179
ACYS238
ACYS242
BCYS176
BHIS179
BCYS238
BCYS242

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
ChainResidueDetails
ALYS120
BLYS120

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171
ChainResidueDetails
ALYS120
BLYS120

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
ChainResidueDetails
ASER183
ASER269
BSER183
BSER269

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
ChainResidueDetails
ATHR284
BTHR284

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:12724314
ChainResidueDetails
ALYS305
BLYS305

site_idSWS_FT_FI8
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131
ChainResidueDetails
ALYS291
ALYS292
BLYS291
BLYS292

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PDB entries from 2024-07-10

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