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 | 5 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | 60M407 |
| A | HOH501 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | HOH606 |
| A | ARG172 |
| A | VAL179 |
| A | ILE180 |
| A | THR181 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | TRP53 |
| A | ARG102 |
| A | HOH523 |
| A | HOH530 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | ARG209 |
| A | ARG252 |
| A | ALA275 |
| A | ARG276 |
| A | ALA289 |
| A | GLY290 |
| A | ALA291 |
| A | LYS297 |
| A | HOH541 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | ARG209 |
| A | ARG252 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | ARG130 |
| A | ARG148 |
| A | ASP152 |
| A | ASP171 |
| A | ARG172 |
| A | ILE173 |
| A | HOH537 |
| A | HOH621 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue 60M A 407 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | ASP120 |
| A | HIS121 |
| A | HIS196 |
| A | SER221 |
| A | SER225 |
| A | HIS263 |
| A | ALA266 |
| A | ZN401 |
| A | HOH501 |
| A | HOH511 |
| A | HOH578 |
| A | HOH626 |
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 | 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 | TYR229 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS263 | metal ligand |
