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
Chain | GOid | namespace | contents |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0005634 | cellular_component | nucleus |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0006915 | biological_process | apoptotic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 301 |
Chain | Residue |
A | PRO177 |
A | HIS178 |
A | ARG181 |
A | CYS182 |
A | GLY244 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | MET169 |
A | THR170 |
A | GLU171 |
A | GLU198 |
A | HOH482 |
A | THR140 |
A | SER166 |
A | GLN167 |
A | HIS168 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | ASN131 |
A | PRO152 |
A | ASP259 |
A | SER260 |
A | SER261 |
A | HOH405 |
A | HOH484 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | GLY154 |
A | THR155 |
A | ARG156 |
A | PRO219 |
A | EDO305 |
A | EDO306 |
A | HOH426 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | LYS101 |
A | THR102 |
A | GLY154 |
A | SER260 |
A | EDO304 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 306 |
Chain | Residue |
A | PRO151 |
A | PRO152 |
A | PRO153 |
A | THR155 |
A | TYR220 |
A | PRO222 |
A | EDO304 |
A | HOH498 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 307 |
Chain | Residue |
A | GLU180 |
A | ARG181 |
A | SER183 |
A | PRO191 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 308 |
Chain | Residue |
A | CYS176 |
A | HIS179 |
A | CYS238 |
A | CYS242 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 190 |
Details | DNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
Chain | Residue | Details |
A | THR102-LYS292 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | CYS176 | |
A | HIS179 | |
A | CYS238 | |
A | CYS242 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
Chain | Residue | Details |
A | LYS120 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-lactoyllysine => ECO:0000269|PubMed:38653238 |
Chain | Residue | Details |
A | LYS120 | |
A | LYS139 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 |
Chain | Residue | Details |
A | SER183 | |
A | SER269 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 |
Chain | Residue | Details |
A | THR284 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131 |
Chain | Residue | Details |
A | LYS291 | |
A | LYS292 |