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 |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046677 | biological_process | response to antibiotic |
| D | 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 2001 |
| Chain | Residue |
| A | HIS121 |
| A | HIS263 |
| A | ZN2002 |
| A | HOH2095 |
| A | HOH2096 |
| A | HOH2108 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 2002 |
| Chain | Residue |
| A | ZN2001 |
| A | HOH2095 |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | HIS121 |
| B | HIS263 |
| B | HOH2084 |
| B | HOH2085 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2002 |
| Chain | Residue |
| B | HIS116 |
| B | HIS118 |
| B | HIS196 |
| B | HOH2084 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 2001 |
| Chain | Residue |
| C | HIS121 |
| C | HIS263 |
| C | HOH2069 |
| C | HOH2070 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 2002 |
| Chain | Residue |
| C | HIS116 |
| C | HIS118 |
| C | HIS196 |
| C | HOH2069 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 2001 |
| Chain | Residue |
| D | HIS121 |
| D | HIS263 |
| D | HOH2093 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 2002 |
| Chain | Residue |
| D | HIS116 |
| D | HIS118 |
| D | HIS196 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 | ASN120 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| B | ASN120 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| C | ASN120 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| D | ASN120 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | ASN120 | metal ligand |
| A | HIS121 | metal ligand |
| A | HIS196 | metal ligand |
| A | TYR228 | 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 | ASN120 | metal ligand |
| B | HIS121 | metal ligand |
| B | HIS196 | metal ligand |
| B | TYR228 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS263 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| C | HIS116 | metal ligand |
| C | HIS118 | metal ligand |
| C | ASN120 | metal ligand |
| C | HIS121 | metal ligand |
| C | HIS196 | metal ligand |
| C | TYR228 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS263 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 258 |
| Chain | Residue | Details |
| D | HIS116 | metal ligand |
| D | HIS118 | metal ligand |
| D | ASN120 | metal ligand |
| D | HIS121 | metal ligand |
| D | HIS196 | metal ligand |
| D | TYR228 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS263 | metal ligand |
