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5MCU

New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LHG2)

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 Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS176
AHIS179
ACYS238
ACYS242

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 302
ChainResidue
AGLU285
AHOH405
ALYS132
ASER240
APRO250
AVAL272
AARG273

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
APHE113
ALEU114
ACYS124
AMET133
APRO142

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 304
ChainResidue
AASP207
AARG209
AHOH420
BASN263

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS176
BHIS179
BCYS238
BCYS242

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO B 302
ChainResidue
BLYS132
BSER240
BPRO250
BVAL272
BARG273
BGLU285
BHOH405

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BPHE113
BLEU114
BCYS124
BMET133
BPRO142

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO B 304
ChainResidue
AASN263
BASP207
BHOH425

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 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 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 2025-06-18

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