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 1 |
| Chain | Residue |
| A | ASP120 |
| A | CYS221 |
| A | HIS263 |
| A | SDF311 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 2 |
| Chain | Residue |
| A | HOH330 |
| A | HOH365 |
| A | HOH28 |
| A | THR181 |
| A | LEU182 |
| A | GLN183 |
| A | GLU184 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 3 |
| Chain | Residue |
| A | ASP179 |
| A | ARG188 |
| A | PHE190 |
| A | HOH332 |
| A | HOH423 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 308 |
| Chain | Residue |
| A | HIS176 |
| A | ASP177 |
| A | GLY178 |
| A | ASP179 |
| A | HOH524 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 309 |
| Chain | Residue |
| A | HOH64 |
| A | HOH64 |
| A | ARG140 |
| A | ARG140 |
| A | ARG143 |
| A | ARG143 |
| A | HOH362 |
| A | HOH362 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 310 |
| Chain | Residue |
| A | LYS97 |
| A | ARG102 |
| A | HOH214 |
| A | LYS257 |
| A | HOH324 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | ARG143 |
| A | ARG143 |
| A | LYS147 |
| A | LYS147 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 5 |
| Chain | Residue |
| A | LYS129 |
| A | VAL170 |
| A | LEU171 |
| A | HOH270 |
| A | LYS302 |
| A | HOH410 |
| A | HOH450 |
| A | HOH495 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SDF A 311 |
| Chain | Residue |
| A | ZN1 |
| A | VAL67 |
| A | TRP87 |
| A | ASP120 |
| A | HIS196 |
| A | CYS221 |
| A | LYS224 |
| A | GLY232 |
| A | ASN233 |
| A | HIS263 |
| A | HOH347 |
| A | HOH419 |
| A | HOH473 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. InTNyHTDraGGnaywksi.G |
| Chain | Residue | Details |
| A | ILE113-GLY133 | |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PdeqVLyGgCILK |
| Chain | Residue | Details |
| A | PRO209-LYS224 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP120 | |
| A | CYS221 | |
| A | HIS263 | |
| Chain | Residue | Details |
| A | THR157 | |
| Chain | Residue | Details |
| A | HIS196 | |
| Chain | Residue | Details |
| A | LYS224 | |
| Chain | Residue | Details |
| A | ASN233 | |
