Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4AGL

Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan784

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 P84 A 400
ChainResidue
ALEU145
AVAL147
ATHR150
AGLU221
APRO222
APRO223
ATHR230
AHOH2110

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1300
ChainResidue
AHIS179
ACYS238
ACYS242
ACYS176

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE P84 B 400
ChainResidue
BLEU145
BVAL147
BTHR150
BGLU221
BPRO222
BPRO223
BHOH2093

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1300
ChainResidue
BCYS176
BHIS179
BCYS238
BCYS242

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 Residues4
DetailsMOD_RES: N6-lactoyllysine => ECO:0000269|PubMed:38653238
ChainResidueDetails
ALYS120
ALYS139
BLYS120
BLYS139

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon