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 | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | SER70 |
| A | SER130 |
| A | LYS234 |
| A | THR235 |
| A | GLY236 |
| A | THR237 |
| A | HOH2152 |
| A | HOH2153 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMQSVfKlhlAMLVL |
| Chain | Residue | Details |
| A | PHE66-LEU81 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10825176","evidenceCode":"ECO:0000303"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A5R8T042","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | GLU166 | |
| A | LYS73 | |
| A | SER130 | |
| A | SER70 | |
