Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0042597 | cellular_component | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 270 |
| Chain | Residue |
| A | ASP88 |
| A | HIS89 |
| A | HIS225 |
| A | ZN271 |
| A | HOH528 |
| A | HOH568 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 271 |
| Chain | Residue |
| A | ZN270 |
| A | HOH528 |
| A | HOH568 |
| A | HIS84 |
| A | HIS86 |
| A | HIS160 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 21 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG |
| Chain | Residue | Details |
| A | LEU81-GLY101 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS84 | |
| A | HIS86 | |
| A | ASP88 | |
| A | HIS89 | |
| A | HIS160 | |
| Chain | Residue | Details |
| A | ASP184 | |
| Chain | Residue | Details |
| A | HIS225 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 10433708, 9811546 |
| Chain | Residue | Details |
| A | TYR191 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| A | HIS84 | metal ligand |
| A | HIS86 | metal ligand |
| A | ASP88 | metal ligand |
| A | HIS89 | metal ligand |
| A | HIS160 | metal ligand |
| A | TYR191 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS225 | metal ligand |
