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 | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 314 |
| Chain | Residue |
| A | MX11 |
| A | ASP120 |
| A | HIS121 |
| A | HIS263 |
| A | ZN315 |
| A | HOH600 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 315 |
| Chain | Residue |
| A | HIS196 |
| A | ZN314 |
| A | HOH600 |
| A | MX11 |
| A | HIS116 |
| A | HIS118 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 316 |
| Chain | Residue |
| A | ARG172 |
| A | VAL179 |
| A | ILE180 |
| A | THR181 |
| A | HOH594 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE MX1 A 1 |
| Chain | Residue |
| A | TYR32 |
| A | TRP38 |
| A | HIS116 |
| A | HIS118 |
| A | ASP120 |
| A | HIS121 |
| A | PHE156 |
| A | ILE162 |
| A | HIS196 |
| A | SER221 |
| A | SER223 |
| A | PRO226 |
| A | HIS263 |
| A | ZN314 |
| A | ZN315 |
| A | HOH328 |
| A | HOH480 |
| A | HOH573 |
| A | HOH581 |
| A | HOH600 |
| A | HOH607 |
| A | HOH611 |
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 | LEU113-GLY133 | |
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 | ASP120 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | ASP120 | metal ligand |
| A | HIS121 | metal ligand |
| A | HIS196 | metal ligand |
| A | TYR228 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS263 | metal ligand |
