9OR3
X-ray diffraction structure of CTX-M-14 beta-lactamase co-crystallized with avibactam
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0005576 | cellular_component | extracellular region |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMCSTsKvmaAAAVL |
| Chain | Residue | Details |
| A | PHE66-LEU81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"UniProtKB","id":"A0A5R8T042","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10101","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A5R8T042","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
