4IBZ
Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R
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 |
| B | 0000976 | molecular_function | transcription cis-regulatory region binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006915 | biological_process | apoptotic process |
| C | 0000976 | molecular_function | transcription cis-regulatory region binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006915 | biological_process | apoptotic process |
| D | 0000976 | molecular_function | transcription cis-regulatory region binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006915 | biological_process | apoptotic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | CYS176 |
| A | HIS179 |
| A | CYS238 |
| A | CYS242 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | THR170 |
| A | VAL172 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | ILE254 |
| A | THR256 |
| A | HOH433 |
| A | HOH439 |
| A | ARG158 |
| A | ALA159 |
| A | MET160 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | ASP186 |
| A | ARG196 |
| A | VAL197 |
| A | GLU198 |
| A | ASN235 |
| A | MET237 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | THR102 |
| A | HOH555 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | CYS176 |
| B | HIS179 |
| B | CYS238 |
| B | CYS242 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | SER260 |
| B | SER261 |
| B | HOH529 |
| D | ALA119 |
| D | LYS120 |
| D | HOH435 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| B | ASP207 |
| B | HOH470 |
| B | HOH506 |
| D | LEU114 |
| D | HIS115 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | PRO190 |
| B | PRO191 |
| B | GLN192 |
| B | HIS193 |
| B | ASP207 |
| B | HIS214 |
| B | HOH456 |
| D | HIS115 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 305 |
| Chain | Residue |
| B | PHE113 |
| B | HIS115 |
| B | GLN144 |
| B | HOH541 |
| D | EDO302 |
| D | EDO306 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 306 |
| Chain | Residue |
| B | MET160 |
| B | LEU206 |
| B | ASP208 |
| B | THR211 |
| B | ARG213 |
| B | HIS214 |
| B | SER215 |
| B | HOH503 |
| B | HOH562 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 307 |
| Chain | Residue |
| B | ARG110 |
| B | HOH505 |
| D | EDO302 |
| D | EDO307 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | CYS176 |
| C | HIS179 |
| C | CYS238 |
| C | CYS242 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | PRO98 |
| C | ARG158 |
| C | MET160 |
| C | ILE254 |
| C | THR256 |
| C | HOH437 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 303 |
| Chain | Residue |
| A | LEU114 |
| A | HIS115 |
| A | SER116 |
| C | ASP207 |
| C | ARG209 |
| C | HOH496 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 304 |
| Chain | Residue |
| A | ALA119 |
| C | SER261 |
| C | GLY262 |
| C | HOH467 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 305 |
| Chain | Residue |
| C | ARG209 |
| C | ASN210 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | CYS176 |
| D | HIS179 |
| D | CYS238 |
| D | CYS242 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 302 |
| Chain | Residue |
| B | HIS115 |
| B | TRP146 |
| B | EDO305 |
| B | ACT307 |
| D | PRO191 |
| D | GLN192 |
| D | EDO307 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 303 |
| Chain | Residue |
| D | THR125 |
| D | TYR126 |
| D | HOH434 |
| D | HOH527 |
| D | LEU114 |
| D | SER116 |
| D | CYS124 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 304 |
| Chain | Residue |
| D | SER240 |
| D | ARG248 |
| D | CYS273 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 305 |
| Chain | Residue |
| D | MET160 |
| D | LEU206 |
| D | ASP208 |
| D | THR211 |
| D | ARG213 |
| D | HIS214 |
| D | SER215 |
| D | HOH442 |
| D | HOH520 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 306 |
| Chain | Residue |
| B | LEU114 |
| B | HIS115 |
| B | EDO305 |
| D | ASP207 |
| D | HOH432 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 307 |
| Chain | Residue |
| B | TRP146 |
| B | ACT307 |
| D | GLU180 |
| D | PRO191 |
| D | EDO302 |
| D | HOH526 |
| D | HOH541 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 308 |
| Chain | Residue |
| D | GLY187 |
| D | HOH450 |
| D | HOH482 |
Functional Information from PROSITE/UniProt
| site_id | PS00348 |
| Number of Residues | 13 |
| Details | P53 p53 family signature. MCNSSCMGGMNRR |
| Chain | Residue | Details |
| A | MET237-ARG249 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 760 |
| Details | DNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
| Chain | Residue | Details |
| A | THR102-LYS292 | |
| B | THR102-LYS292 | |
| C | THR102-LYS292 | |
| D | THR102-LYS292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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 | |
| C | HIS179 | |
| C | CYS238 | |
| C | CYS242 | |
| D | CYS176 | |
| D | HIS179 | |
| D | CYS238 | |
| D | CYS242 | |
| A | HIS179 | |
| A | CYS238 | |
| A | CYS242 | |
| B | CYS176 | |
| B | HIS179 | |
| B | CYS238 | |
| B | CYS242 | |
| C | CYS176 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 |
| Chain | Residue | Details |
| A | LYS120 | |
| B | LYS120 | |
| C | LYS120 | |
| D | LYS120 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-lactoyllysine => ECO:0000269|PubMed:38653238 |
| Chain | Residue | Details |
| A | LYS120 | |
| A | LYS139 | |
| B | LYS120 | |
| B | LYS139 | |
| C | LYS120 | |
| C | LYS139 | |
| D | LYS120 | |
| D | LYS139 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 |
| Chain | Residue | Details |
| A | SER183 | |
| A | SER269 | |
| B | SER183 | |
| B | SER269 | |
| C | SER183 | |
| C | SER269 | |
| D | SER183 | |
| D | SER269 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 |
| Chain | Residue | Details |
| A | ARG284 | |
| B | ARG284 | |
| C | ARG284 | |
| D | ARG284 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131 |
| Chain | Residue | Details |
| A | LYS291 | |
| D | LYS291 | |
| D | LYS292 | |
| A | LYS292 | |
| B | LYS291 | |
| B | LYS292 | |
| C | LYS291 | |
| C | LYS292 |
