4KG5
Crystal Structure of AmpC beta-lactamase N152G Mutant in Complex with Cefotaxime
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 (B, A, C, D) | Beta-lactamase | polymer | 358 | 39530.9 | 4 | UniProt (P00811) Pfam (PF00144) | Escherichia coli | Cephalosporinase |
| 2 | E, G, H, I, L (B, A, D) | PHOSPHATE ION | non-polymer | 95.0 | 5 | Chemie (PO4) | |||
| 3 | F, J, K, M (B, A, C, D) | CEFOTAXIME, C3' cleaved, open, bound form | non-polymer | 397.4 | 4 | Chemie (CEF) | |||
| 4 | N, O, P, Q (B, A, C, D) | water | water | 18.0 | 496 | Chemie (HOH) |
Sequence modifications
B, A, C, D: 4 - 361 (UniProt: P00811)
| PDB | External Database | Details |
|---|---|---|
| Gly 152 | Asn 168 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 158123.5 | |
| Non-Polymers* | Number of molecules | 9 |
| Total formula weight | 2064.6 | |
| All* | Total formula weight | 160188.1 |
