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 |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SR A 401 |
| Chain | Residue |
| A | ASP87 |
| B | ASP58 |
| B | HOH523 |
| B | HOH628 |
| B | HOH636 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SR A 402 |
| Chain | Residue |
| A | HOH577 |
| A | HOH655 |
| A | ASP219 |
| A | ASP220 |
| A | HOH517 |
| A | HOH571 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SR A 403 |
| Chain | Residue |
| A | ASP291 |
| A | GLU295 |
| A | GLU352 |
| A | HOH524 |
| A | HOH525 |
| A | HOH656 |
| A | HOH659 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 404 |
| Chain | Residue |
| A | VAL122 |
| A | HOH539 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SR B 401 |
| Chain | Residue |
| B | ASP219 |
| B | ASP220 |
| B | HOH515 |
| B | HOH525 |
| B | HOH549 |
| B | HOH629 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SR B 402 |
| Chain | Residue |
| B | ASP291 |
| B | GLU295 |
| B | GLU352 |
| B | HOH611 |
| B | HOH632 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 403 |
| Chain | Residue |
| B | VAL122 |
| B | ASN153 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SR C 401 |
| Chain | Residue |
| A | ASP128 |
| C | ASP58 |
| C | HOH665 |
| C | HOH691 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SR C 402 |
| Chain | Residue |
| C | ASP219 |
| C | ASP220 |
| C | HOH539 |
| C | HOH617 |
| C | HOH636 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SR C 403 |
| Chain | Residue |
| C | ASP291 |
| C | GLU295 |
| C | GLU352 |
| C | HOH528 |
| C | HOH529 |
| C | HOH532 |
| C | HOH533 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 404 |
| Chain | Residue |
| C | VAL122 |
| C | ASN153 |
| C | HOH562 |
Functional Information from PROSITE/UniProt
| site_id | PS00336 |
| Number of Residues | 8 |
| Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSLSK |
| Chain | Residue | Details |
| A | PHE61-LYS68 | |
