Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| 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 |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue EPE A 301 |
| Chain | Residue |
| A | SER70 |
| A | HOH492 |
| A | HOH541 |
| A | SER130 |
| A | LYS234 |
| A | THR235 |
| A | GLY236 |
| A | ALA237 |
| A | ARG244 |
| A | TYR274 |
| A | EPE303 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | SER87 |
| A | ILE88 |
| A | GLU202 |
| A | LYS203 |
| A | ASP275 |
| A | LYS277 |
| A | HOH529 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue EPE A 303 |
| Chain | Residue |
| A | SER70 |
| A | ASN104 |
| A | ASN132 |
| A | ASN170 |
| A | ALA237 |
| A | ALA238 |
| A | EPE301 |
| A | HOH433 |
| A | HOH439 |
| A | HOH492 |
| B | ASP114 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue EPE B 301 |
| Chain | Residue |
| A | HOH421 |
| B | SER70 |
| B | SER130 |
| B | LYS234 |
| B | THR235 |
| B | GLY236 |
| B | ALA237 |
| B | ARG244 |
| B | EPE303 |
| B | HOH477 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ILE88 |
| B | GLU202 |
| B | LYS203 |
| B | ASP275 |
| B | LYS277 |
| B | HOH480 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue EPE B 303 |
| Chain | Residue |
| A | ASP114 |
| B | SER70 |
| B | ASN104 |
| B | ASN132 |
| B | ASN170 |
| B | ALA237 |
| B | EPE301 |
| B | HOH466 |
| B | HOH477 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FALDTGTNRTVA |
| Chain | Residue | Details |
| A | PHE47-ALA59 | |
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFASTiKaltVGVLL |
| 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":"P62593","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P62593","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
5ZFL
