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4IBW

Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R 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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS176
AHIS179
ACYS238
ACYS242

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
ASER95
ATHR231
AHIS233
AHOH659

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASP148
AASP208
AASN210
AEDO306
AHOH465
AHOH559
AHOH658
AHOH683
AARG110

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AGLU224
AVAL225
AHOH518
AHOH633
AHOH673

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AARG110
ALEU111
ATRP146
AHOH555
AHOH607

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AARG110
ATRP146
AVAL147
AASP148
AASP228
AEDO303
AHOH456
AHOH575
AHOH658
AHOH686

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
ALEU114
ASER166
AMET169
AHIS233
AHOH498
AHOH536

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
APHE113
ALEU114
AHIS115
ATYR126
APRO128
AARG282
AHOH466
AHOH477
AHOH532
AHOH622

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 309
ChainResidue
ALYS132
ASER240
AARG248
APRO250
AGLU271
AVAL272
AHIS273
AHOH507

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 310
ChainResidue
AASP186
AARG196
AASN235
AHOH669

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 311
ChainResidue
AALA138
ALYS139
ATHR140
AGLN167
AGLU198
AASN235
AHOH655

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 312
ChainResidue
ACYS229
ATHR231
AHOH470
AHOH548

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 313
ChainResidue
ASER94
ASER95
ASER96
AASN200
ALEU201
AEDO315
AHOH594
AHOH679

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 314
ChainResidue
ALYS120
AARG280
AARG283
AHOH464
AHOH547
BDG3
BHOH227

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 315
ChainResidue
ASER95
AGLU221
ATHR230
ATHR231
AEDO313
AHOH492
AHOH634

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 316
ChainResidue
AGLU286
AGLU287
AARG283

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 101
ChainResidue
AARG248
BDT7
BDG8
BEDO102
BHOH241

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 102
ChainResidue
ASER241
AARG248
BDC9
BEDO101
BHOH213
BHOH219
BHOH223

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 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; by KAT6A => 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
AARG284

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

220113

PDB entries from 2024-05-22

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