Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 3 |
| Chain | Residue |
| A | TRP93 |
| A | LEU157 |
| A | LEU161 |
| A | LYS164 |
| A | HOH524 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 362 |
| Chain | Residue |
| A | ARG80 |
| A | HOH551 |
| A | HOH1152 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 363 |
| Chain | Residue |
| A | LYS290 |
| A | HOH404 |
| B | TYR40 |
| B | GLN56 |
| A | ASN289 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 364 |
| Chain | Residue |
| A | ILE33 |
| A | GLY36 |
| A | PRO38 |
| A | ALA231 |
| A | ARG232 |
| A | GLN235 |
| A | HOH570 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3GV A 1 |
| Chain | Residue |
| A | GLY63 |
| A | SER64 |
| A | TYR150 |
| A | ASN152 |
| A | TYR221 |
| A | ASP288 |
| A | ASN289 |
| A | LYS290 |
| A | ILE291 |
| A | LYS315 |
| A | THR316 |
| A | GLY317 |
| A | ALA318 |
| A | ASN346 |
| A | HOH517 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 365 |
| Chain | Residue |
| A | GLY263 |
| A | PRO297 |
| A | VAL298 |
| A | LYS299 |
| B | TYR45 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS B 1 |
| Chain | Residue |
| B | LEU157 |
| B | LEU161 |
| B | LYS164 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS B 362 |
| Chain | Residue |
| B | SER64 |
| B | TYR150 |
| B | THR316 |
| B | ALA318 |
| B | HOH758 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS B 363 |
| Chain | Residue |
| A | PHE41 |
| A | THR42 |
| B | GLY116 |
| B | PRO118 |
| B | TRP142 |
| B | HOH488 |
Functional Information from PROSITE/UniProt
| site_id | PS00336 |
| Number of Residues | 8 |
| Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK |
| Chain | Residue | Details |
| A | PHE60-LYS67 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | SER64 | |
| B | SER64 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR150 | |
| B | TYR150 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS315 | |
| B | LYS315 | |
