4JN4
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
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) | Chaperone protein DnaK | polymer | 608 | 65893.3 | 2 | UniProt (P0A6Y8) Pfam (PF00012) | Escherichia coli | |
| 2 | C, L (A, B) | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
| 3 | D, M (A, B) | ADENOSINE-5'-TRIPHOSPHATE | non-polymer | 507.2 | 2 | Chemie (ATP) | |||
| 4 | E, F, G, H, I... (A, B) | SULFATE ION | non-polymer | 96.1 | 11 | Chemie (SO4) | |||
| 5 | J, K, T, U (A, B) | GLYCEROL | non-polymer | 92.1 | 4 | Chemie (GOL) | |||
| 6 | V, W (A, B) | water | water | 18.0 | 1086 | Chemie (HOH) |
Sequence modifications
A, B: 2 - 610 (UniProt: P0A6Y8)
| PDB | External Database | Details |
|---|---|---|
| Ser 1 | - | expression tag |
| Ala 199 | Thr 199 | conflict |
| - | Thr 428 | deletion |
| - | Ala 429 | deletion |
| - | Glu 430 | deletion |
| - | Asp 431 | deletion |
| Met 428 | Asn 432 | engineered mutation |
| Gly 429 | Gln 433 | engineered mutation |
| Gly 430 | Ser 434 | engineered mutation |
| His 611 | - | expression tag |
| Ala 612 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 131786.7 | |
| Non-Polymers* | Number of molecules | 19 |
| Total formula weight | 2488.0 | |
| All* | Total formula weight | 134274.7 |
