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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | ZN402 |
| A | VII1410 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | VII1410 |
| A | HOH1551 |
| A | ASP120 |
| A | HIS121 |
| A | HIS263 |
| A | ZN401 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS116 |
| B | HIS118 |
| B | HIS196 |
| B | ZN402 |
| B | VII2410 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | ASP120 |
| B | HIS121 |
| B | HIS263 |
| B | ZN401 |
| B | VII2410 |
| B | HOH2540 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1006 |
| Chain | Residue |
| B | ARG172 |
| B | VAL179 |
| B | ILE180 |
| B | THR181 |
| B | HOH2542 |
| B | HOH2588 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1007 |
| Chain | Residue |
| A | ARG172 |
| A | VAL179 |
| A | ILE180 |
| A | THR181 |
| A | PEG1005 |
| A | HOH1615 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1008 |
| Chain | Residue |
| A | ARG252 |
| A | LYS297 |
| A | HOH1634 |
| B | ARG209 |
| B | ALA275 |
| B | ARG276 |
| B | ALA289 |
| B | GLY290 |
| B | ALA291 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE VII A 1410 |
| Chain | Residue |
| A | TRP39 |
| A | HIS116 |
| A | HIS118 |
| A | ASP120 |
| A | HIS121 |
| A | PHE156 |
| A | ILE162 |
| A | HIS196 |
| A | SER225 |
| A | PRO227 |
| A | HIS263 |
| A | ZN401 |
| A | ZN402 |
| A | HOH1551 |
| A | HOH1573 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE VII B 2410 |
| Chain | Residue |
| B | TRP39 |
| B | HIS116 |
| B | HIS118 |
| B | ASP120 |
| B | HIS121 |
| B | PHE156 |
| B | ILE162 |
| B | HIS196 |
| B | SER225 |
| B | HIS263 |
| B | ZN401 |
| B | ZN402 |
| B | HOH2540 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 1001 |
| Chain | Residue |
| A | ASN169 |
| B | VAL144 |
| B | ARG148 |
| B | ALA170 |
| B | ILE173 |
| B | HOH2478 |
| B | HOH2538 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 1002 |
| Chain | Residue |
| A | ARG148 |
| A | ASP152 |
| A | ASP171 |
| B | PRO166 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 1004 |
| Chain | Residue |
| A | ARG107 |
| B | ARG172 |
| B | HOH2536 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 1005 |
| Chain | Residue |
| A | ARG110 |
| A | THR181 |
| A | SO41007 |
| A | HOH1564 |
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 | 10 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| B | 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 | TYR229 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS263 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| B | HIS116 | metal ligand |
| B | HIS118 | metal ligand |
| B | ASP120 | metal ligand |
| B | HIS121 | metal ligand |
| B | HIS196 | metal ligand |
| B | TYR229 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS263 | metal ligand |
