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4IBV

Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation S240R in sequence-specific complex with DNA

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
APRO177
AHIS178
AARG181
ACYS182
AGLY244

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AMET169
ATHR170
AGLU171
AGLU198
AHOH482
ATHR140
ASER166
AGLN167
AHIS168

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASN131
APRO152
AASP259
ASER260
ASER261
AHOH405
AHOH484

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AGLY154
ATHR155
AARG156
APRO219
AEDO305
AEDO306
AHOH426

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ALYS101
ATHR102
AGLY154
ASER260
AEDO304

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
APRO151
APRO152
APRO153
ATHR155
ATYR220
APRO222
AEDO304
AHOH498

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
AGLU180
AARG181
ASER183
APRO191

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 308
ChainResidue
ACYS176
AHIS179
ACYS238
ACYS242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues190
DetailsDNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
ChainResidueDetails
ATHR102-LYS292

site_idSWS_FT_FI2
Number of Residues4
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

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
ChainResidueDetails
ALYS120

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171
ChainResidueDetails
ALYS120

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
ChainResidueDetails
ASER183
ASER269

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
ChainResidueDetails
ATHR284

site_idSWS_FT_FI7
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131
ChainResidueDetails
ALYS292
ALYS291

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PDB entries from 2024-06-12

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