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 | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue ZXM A 401 |
| Chain | Residue |
| A | SER65 |
| A | GLN121 |
| A | TYR151 |
| A | ASN153 |
| A | TYR223 |
| A | GLY314 |
| A | SER315 |
| A | SER316 |
| A | ASN340 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 402 |
| Chain | Residue |
| A | ARG329 |
| A | ALA358 |
| A | GLY359 |
| A | ZN418 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 403 |
| Chain | Residue |
| A | GLU130 |
| A | ARG133 |
| A | HOH590 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue ACT A 404 |
| Chain | Residue |
| A | HIS93 |
| A | TRP96 |
| A | ARG133 |
| A | HIS161 |
| A | SER165 |
| A | ACT405 |
| A | ACT407 |
| A | ZN410 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 405 |
| Chain | Residue |
| A | SER129 |
| A | MET132 |
| A | ARG133 |
| A | HIS161 |
| A | ACT404 |
| A | ACT407 |
| A | ZN410 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 406 |
| Chain | Residue |
| A | HIS259 |
| A | ZN414 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 407 |
| Chain | Residue |
| A | ARG133 |
| A | HIS161 |
| A | ACT404 |
| A | ACT405 |
| A | ZN410 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 408 |
| Chain | Residue |
| A | VAL308 |
| A | PHE310 |
| A | PRO327 |
| A | ZN416 |
| A | HOH545 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 409 |
| Chain | Residue |
| A | LYS206 |
| A | GLU207 |
| A | ZN412 |
| A | HOH519 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 410 |
| Chain | Residue |
| A | HIS161 |
| A | ACT404 |
| A | ACT405 |
| A | ACT407 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 411 |
| Chain | Residue |
| A | HIS186 |
| A | HOH552 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 412 |
| Chain | Residue |
| A | GLU207 |
| A | ACT409 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 413 |
| Chain | Residue |
| A | ASN191 |
| A | HOH537 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 414 |
| Chain | Residue |
| A | HIS259 |
| A | ACT406 |
| A | HOH643 |
| A | HOH657 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 415 |
| Chain | Residue |
| A | GLU50 |
| A | HIS148 |
| A | HOH501 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 416 |
| Chain | Residue |
| A | HIS256 |
| A | ACT408 |
| A | HOH545 |
| A | HOH671 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 417 |
| Chain | Residue |
| A | HIS187 |
| A | ASP231 |
| A | HOH600 |
| A | HOH606 |
| A | HOH630 |
| A | HOH647 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 418 |
| Chain | Residue |
| A | GLY359 |
| A | ACT402 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 419 |
| site_id | AE2 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 420 |
Functional Information from PROSITE/UniProt
| site_id | PS00336 |
| Number of Residues | 8 |
| Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK |
| Chain | Residue | Details |
| A | PHE61-LYS68 | |