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 | 6 |
| Details | BINDING SITE FOR RESIDUE GV9 A 1 |
| Chain | Residue |
| A | SER64 |
| A | GLN120 |
| A | ASN152 |
| A | GLY317 |
| A | ALA318 |
| A | HOH497 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 362 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GV9 A 363 |
| Chain | Residue |
| A | LYS164 |
| A | PRO165 |
| A | HOH702 |
| B | VAL278 |
| B | ASN279 |
| B | PRO280 |
| A | TYR92 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GV9 A 364 |
| Chain | Residue |
| A | VAL125 |
| A | LYS126 |
| A | SER127 |
| A | GLY214 |
| A | ALA215 |
| A | LEU216 |
| A | PEG365 |
| A | HOH366 |
| A | HOH448 |
| A | HOH848 |
| A | HOH849 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG A 365 |
| Chain | Residue |
| A | TRP93 |
| A | LEU131 |
| A | ALA160 |
| A | LYS164 |
| A | GV9364 |
| A | HOH366 |
| B | ASP281 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GV9 B 1 |
| Chain | Residue |
| B | PO43 |
| B | SER64 |
| B | GLN120 |
| B | ASN152 |
| B | GLY317 |
| B | ALA318 |
| B | DMS363 |
| B | HOH421 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2 |
| Chain | Residue |
| A | ARG14 |
| B | ARG80 |
| B | HOH396 |
| B | HOH511 |
| B | HOH956 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 3 |
| Chain | Residue |
| B | GV91 |
| B | ALA318 |
| B | THR319 |
| B | ASN343 |
| B | DMS363 |
| B | HOH746 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS B 362 |
| Chain | Residue |
| B | TRP93 |
| B | LEU131 |
| B | LEU157 |
| B | LYS164 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS B 363 |
| Chain | Residue |
| B | GV91 |
| B | PO43 |
| B | LEU119 |
| B | GLN120 |
| B | LEU293 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 364 |
| Chain | Residue |
| A | ALA141 |
| A | TRP142 |
| B | THR17 |
| B | PRO18 |
| B | GLU21 |
| B | HOH902 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS B 365 |
| Chain | Residue |
| A | GLN56 |
| A | HOH846 |
| B | ASN289 |
| B | LEU293 |
| B | HOH500 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 366 |
| Chain | Residue |
| B | LYS84 |
| B | HOH469 |
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 | |
