3Q01
An induced fit mechanism regulates p53 DNA binding kinetics to confer sequence specificity
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Cellular tumor antigen p53 | polymer | 233 | 26444.9 | 2 | UniProt (P04637) Pfam (PF00870) Pfam (PF07710) | Homo sapiens (human) | Antigen NY-CO-13, Phosphoprotein p53, Tumor suppressor p53 |
| 2 | C, D (A, B) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 3 | E, F (A, B) | water | water | 18.0 | 135 | Chemie (HOH) |
Sequence modifications
A, B: 94 - 291 (UniProt: P04637)
A, B: 322 - 356 (UniProt: P04637)
| PDB | External Database | Details |
|---|---|---|
| Val 135 | Cys 135 | engineered mutation |
| Val 141 | Cys 141 | engineered mutation |
| Tyr 146 | Trp 146 | engineered mutation |
| Ser 182 | Cys 182 | engineered mutation |
| Ala 203 | Val 203 | engineered mutation |
| Pro 209 | Arg 209 | engineered mutation |
| Tyr 229 | Cys 229 | engineered mutation |
| Tyr 233 | His 233 | engineered mutation |
| Phe 234 | Tyr 234 | engineered mutation |
| Lys 235 | Asn 235 | engineered mutation |
| Phe 236 | Tyr 236 | engineered mutation |
| Val 253 | Thr 253 | engineered mutation |
| Asp 268 | Asn 268 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Thr 322 | Pro 322 | engineered mutation |
| Met 323 | Leu 323 | engineered mutation |
| Gln 340 | Met 340 | engineered mutation |
| Arg 344 | Leu 344 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 52889.7 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 130.8 | |
| All* | Total formula weight | 53020.5 |






