1KSF
Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (X) | ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA | polymer | 758 | 84303.8 | 1 | UniProt (P0ABH9) Pfam (PF02861) Pfam (PF00004) Pfam (PF17871) Pfam (PF07724) Pfam (PF10431) | Escherichia coli | endopeptidase Clp ATP-binding; ATP-binding component of serine protease |
| 2 | B, C (X) | MAGNESIUM ION | non-polymer | 24.3 | 2 | Chemie (MG) | |||
| 3 | D (X) | METHIONINE | non-polymer | 149.2 | 1 | Chemie (MET) | |||
| 4 | E, F (X) | TRIETHYLENE GLYCOL | non-polymer | 150.2 | 2 | Chemie (PGE) | |||
| 5 | G, H (X) | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 2 | Chemie (ADP) | |||
| 6 | I, J, K, L, M (X) | ISOPROPYL ALCOHOL | non-polymer | 60.1 | 5 | Chemie (IPA) | |||
| 7 | N (X) | water | water | 18.0 | 242 | Chemie (HOH) |
Sequence modifications
X: 1 - 758 (UniProt: P0ABH9)
| PDB | External Database | Details |
|---|---|---|
| Leu 169 | Met 169 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 84303.8 | |
| Non-Polymers* | Number of molecules | 12 |
| Total formula weight | 1653.0 | |
| All* | Total formula weight | 85956.9 |
