3Q05
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, C, D (A, C, D, B) | Cellular tumor antigen p53 | polymer | 234 | 26618.1 | 4 | UniProt (P04637) Pfam (PF00870) Pfam (PF07710) | Homo sapiens (human) | Antigen NY-CO-13, Phosphoprotein p53, Tumor suppressor p53 |
| 2 | E (K) | DNA (26-MER) | polymer | 26 | 7948.1 | 1 | |||
| 3 | F (L) | DNA (26-MER) | polymer | 26 | 8028.2 | 1 | |||
| 4 | G, H, I, J (A, C, D, B) | ZINC ION | non-polymer | 65.4 | 4 | Chemie (ZN) | |||
| 5 | K, L, M, N, O... (A, C, D, B, K...) | water | water | 18.0 | 161 | Chemie (HOH) |
Sequence modifications
A, C, D, B: 94 - 291 (UniProt: P04637)
A, C, D, B: 321 - 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 |
| Thr 356 | Gly 356 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 6 |
| Total formula weight | 122448.7 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 261.6 | |
| All* | Total formula weight | 122710.3 |
