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 |
| 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 | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue SM2 A 400 |
| Chain | Residue |
| A | SER64 |
| A | HOH584 |
| A | HOH625 |
| A | HOH647 |
| A | HOH651 |
| A | HOH681 |
| A | HOH710 |
| A | HOH780 |
| A | GLN120 |
| A | TYR150 |
| A | ASN152 |
| A | TYR222 |
| A | GLY316 |
| A | SER317 |
| A | THR318 |
| A | GLY319 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS160 |
| A | HOH635 |
| A | HOH818 |
| A | HOH829 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HIS39 |
| A | HOH540 |
| A | HOH807 |
| A | HOH836 |
| B | ASP274 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 403 |
| Chain | Residue |
| A | GLU124 |
| A | ASP126 |
| B | HIS147 |
| B | HOH776 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 404 |
| Chain | Residue |
| A | HIS185 |
| A | HOH771 |
| A | HOH837 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 405 |
| Chain | Residue |
| A | HIS160 |
| A | LEU217 |
| A | GLU220 |
| A | HOH537 |
| A | HOH741 |
| A | HOH839 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | HIS160 |
| B | ACT408 |
| B | HOH746 |
| B | HOH808 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| A | ASP274 |
| B | HIS39 |
| B | ACT409 |
| B | HOH557 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 403 |
| Chain | Residue |
| A | HIS147 |
| B | GLU124 |
| B | ASP126 |
| B | ACT406 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 404 |
| Chain | Residue |
| B | HIS185 |
| B | HOH781 |
| B | HOH804 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 405 |
| Chain | Residue |
| B | HIS160 |
| B | LEU217 |
| B | GLU220 |
| B | HOH539 |
| B | HOH771 |
| B | HOH774 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue ACT B 406 |
| Chain | Residue |
| A | TYR142 |
| A | HIS147 |
| A | ALA294 |
| A | PRO296 |
| B | GLU124 |
| B | ASP126 |
| B | LYS130 |
| B | ZN403 |
| B | HOH530 |
| B | HOH665 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 407 |
| Chain | Residue |
| A | GLU361 |
| B | HIS186 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 408 |
| Chain | Residue |
| B | HIS92 |
| B | TRP95 |
| B | HIS160 |
| B | LEU161 |
| B | ASN164 |
| B | ZN401 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 409 |
| Chain | Residue |
| A | ASP274 |
| B | THR9 |
| B | HIS39 |
| B | ZN402 |
| B | HOH557 |
| B | HOH561 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 410 |
| Chain | Residue |
| A | HIS186 |
| B | GLU361 |
| B | HOH725 |
| site_id | AD8 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide SM2 B 400 and SER B 64 |
| Chain | Residue |
| B | GLY316 |
| B | SER317 |
| B | THR318 |
| B | GLY319 |
| B | HOH507 |
| B | HOH509 |
| B | HOH604 |
| B | HOH646 |
| B | HOH671 |
| B | ILE62 |
| B | GLY63 |
| B | VAL65 |
| B | SER66 |
| B | LYS67 |
| B | GLN120 |
| B | TYR150 |
| B | ASN152 |
| B | ALA221 |
| B | TYR222 |
| B | PHE292 |
| B | LYS314 |
| B | THR315 |
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 | PHE60-LYS67 | |
