1TYF
THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS
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, E... (A, B, C, D, E...) | CLP PEPTIDASE | polymer | 193 | 21586.9 | 14 | UniProt (P0A6G7) Pfam (PF00574) | Escherichia coli | CLPP |
| 2 | AA, BA, O, P, Q... (M, N, A, B, C...) | water | water | 18.0 | 1246 | Chemie (HOH) |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 14 |
| Total formula weight | 302216.1 | |
| All* | Total formula weight | 302216.1 |
