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 | 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS84 |
| A | HIS86 |
| A | HIS160 |
| A | I38501 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | ASP88 |
| A | HIS89 |
| A | HIS225 |
| A | I38501 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | HIS29 |
| A | HIS29 |
| A | ASP28 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | ARG137 |
| A | VAL144 |
| A | ILE145 |
| A | THR146 |
| A | HOH730 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | ARG173 |
| A | ARG214 |
| A | ALA237 |
| A | ARG238 |
| A | ALA239 |
| A | GLY240 |
| A | ALA241 |
| A | LYS247 |
| A | HOH750 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | GLU95 |
| A | ARG98 |
| A | ARG99 |
| A | HOH834 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE I38 A 501 |
| Chain | Residue |
| A | TYR11 |
| A | ASP88 |
| A | HIS160 |
| A | SER187 |
| A | PRO189 |
| A | ZN401 |
| A | ZN402 |
| A | HOH606 |
| A | HOH610 |
| A | HOH812 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17999929","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9811546","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| A | ASP88 | |
| 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 |
