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 |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE AZI A 1292 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1300 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | ZN1301 |
| A | HOH2258 |
| A | HOH2259 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1301 |
| Chain | Residue |
| A | HIS263 |
| A | GOL1295 |
| A | ZN1300 |
| A | HOH2258 |
| A | ASP120 |
| A | CYS221 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1302 |
| Chain | Residue |
| A | SER225 |
| A | THR226 |
| A | SER227 |
| A | GLY264 |
| A | GLU265 |
| A | HOH2260 |
| A | HOH2261 |
| A | HOH2263 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AZI B 1292 |
| Chain | Residue |
| B | HIS196 |
| B | LYS224 |
| B | GLY232 |
| B | ASN233 |
| B | GOL1297 |
| B | ZN1300 |
| B | HOH2113 |
| B | HOH2177 |
| B | HOH2233 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1299 |
| Chain | Residue |
| B | HIS116 |
| B | HIS118 |
| B | HIS196 |
| B | ZN1300 |
| B | HOH2113 |
| B | HOH2243 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 1300 |
| Chain | Residue |
| B | ASP120 |
| B | CYS221 |
| B | HIS263 |
| B | AZI1292 |
| B | ZN1299 |
| B | HOH2177 |
| B | HOH2243 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1301 |
| Chain | Residue |
| B | VAL177 |
| B | LYS181 |
| B | LYS186 |
| B | ARG252 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1302 |
| Chain | Residue |
| B | SER225 |
| B | THR226 |
| B | SER227 |
| B | GLY264 |
| B | GLU265 |
| B | HOH2246 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1293 |
| Chain | Residue |
| A | THR33 |
| A | LYS103 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1294 |
| Chain | Residue |
| A | LYS148 |
| B | GLU100 |
| B | ARG107 |
| B | ARG131 |
| B | HOH2091 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1295 |
| Chain | Residue |
| A | HIS196 |
| A | CYS221 |
| A | LYS224 |
| A | GLY232 |
| A | ASN233 |
| A | HIS263 |
| A | ZN1301 |
| A | HOH2183 |
| A | HOH2184 |
| A | HOH2259 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1296 |
| Chain | Residue |
| A | ALA117 |
| A | HIS118 |
| A | ALA119 |
| A | ASN149 |
| A | TYR167 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1297 |
| Chain | Residue |
| A | ASP88 |
| A | ASP89 |
| A | LYS90 |
| A | HOH2062 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1298 |
| Chain | Residue |
| A | ASN215 |
| A | HOH2255 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1299 |
| Chain | Residue |
| A | ASN184 |
| A | LYS186 |
| A | GLN210 |
| A | HOH2257 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1303 |
| Chain | Residue |
| B | GLN47 |
| B | LYS50 |
| B | LYS103 |
| B | HOH2039 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1304 |
| Chain | Residue |
| A | GOL1305 |
| B | GLU100 |
| B | GLN105 |
| B | ARG107 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1305 |
| Chain | Residue |
| A | GOL1304 |
| B | ARG107 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1293 |
| Chain | Residue |
| B | ASN215 |
| B | ARG254 |
| B | ASN255 |
| B | HOH2234 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1294 |
| Chain | Residue |
| B | HIS118 |
| B | ALA119 |
| B | TYR167 |
| B | HOH2238 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1295 |
| Chain | Residue |
| B | ASP88 |
| B | ASP89 |
| B | LYS90 |
| B | HOH2117 |
| B | HOH2239 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1296 |
| Chain | Residue |
| B | THR56 |
| B | ASN70 |
| B | GLY264 |
| B | GLU265 |
| B | HOH2022 |
| B | HOH2217 |
| B | HOH2241 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1297 |
| Chain | Residue |
| B | LYS224 |
| B | ASP230 |
| B | LEU231 |
| B | GLY232 |
| B | AZI1292 |
| B | HOH2233 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1298 |
| Chain | Residue |
| B | SER77 |
| B | THR176 |
| B | GLY183 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADciGGiktlker.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. PqynILvGgCLVK |
| Chain | Residue | Details |
| A | PRO209-LYS224 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS116 | |
| A | HIS118 | |
| A | HIS196 | |
| B | HIS116 | |
| B | HIS118 | |
| B | HIS196 | |
| Chain | Residue | Details |
| A | ASP120 | |
| A | CYS221 | |
| A | HIS263 | |
| B | ASP120 | |
| B | CYS221 | |
| B | HIS263 | |
| Chain | Residue | Details |
| A | LYS224 | |
| B | LYS224 | |
| Chain | Residue | Details |
| A | ASN233 | |
| B | ASN233 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP120 | |
| A | ASN233 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP120 | |
| B | ASN233 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP120 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP120 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS196 | metal ligand |
| A | ASN233 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| B | HIS116 | metal ligand |
| B | HIS118 | metal ligand |
| B | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS196 | metal ligand |
| B | ASN233 | electrostatic stabiliser, hydrogen bond donor |
