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2AC0

Structural Basis of DNA Recognition by p53 Tetramers (complex I)

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
C0000976molecular_functiontranscription cis-regulatory region binding
C0003677molecular_functionDNA binding
C0003700molecular_functionDNA-binding transcription factor activity
C0005634cellular_componentnucleus
C0006355biological_processregulation of DNA-templated transcription
C0006915biological_processapoptotic process
D0000976molecular_functiontranscription cis-regulatory region binding
D0003677molecular_functionDNA binding
D0003700molecular_functionDNA-binding transcription factor activity
D0005634cellular_componentnucleus
D0006355biological_processregulation of DNA-templated transcription
D0006915biological_processapoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS176
AHIS179
ACYS238
ACYS242

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BCYS176
BHIS179
BCYS238
BCYS242

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1
ChainResidue
CHIS179
CCYS238
CCYS242
CCYS176

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1
ChainResidue
DCYS176
DHIS179
DCYS238
DCYS242

Functional Information from PROSITE/UniProt
site_idPS00348
Number of Residues13
DetailsP53 p53 family signature. MCNSSCMGGMNRR
ChainResidueDetails
AMET237-ARG249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues760
DetailsDNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
ChainResidueDetails
ATHR102-LYS292
BTHR102-LYS292
CTHR102-LYS292
DTHR102-LYS292

site_idSWS_FT_FI2
Number of Residues16
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
CHIS179
CCYS238
CCYS242
DCYS176
DHIS179
DCYS238
DCYS242
AHIS179
ACYS238
ACYS242
BCYS176
BHIS179
BCYS238
BCYS242
CCYS176

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
ChainResidueDetails
ALYS120
BLYS120
CLYS120
DLYS120

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-lactoyllysine => ECO:0000269|PubMed:38653238
ChainResidueDetails
ALYS120
ALYS139
BLYS120
BLYS139
CLYS120
CLYS139
DLYS120
DLYS139

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
ChainResidueDetails
ASER183
ASER269
BSER183
BSER269
CSER183
CSER269
DSER183
DSER269

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
ChainResidueDetails
ATHR284
BTHR284
CTHR284
DTHR284

site_idSWS_FT_FI7
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131
ChainResidueDetails
ALYS291
DLYS291
DLYS292
ALYS292
BLYS291
BLYS292
CLYS291
CLYS292

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PDB entries from 2024-11-06

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