4ZNB
METALLO-BETA-LACTAMASE (C181S MUTANT)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1 |
| Chain | Residue |
| A | HIS99 |
| A | HIS101 |
| A | ASP103 |
| A | HIS162 |
| A | HOH250 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 3 |
| Chain | Residue |
| A | ASN55 |
| A | ASP69 |
| A | ASP103 |
| A | HOH256 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1 |
| Chain | Residue |
| B | HIS99 |
| B | HIS101 |
| B | HIS162 |
| B | HOH250 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 3 |
| Chain | Residue |
| B | ASN55 |
| B | ASP69 |
| B | ASP103 |
| B | HOH253 |
| site_id | NAA |
| Number of Residues | 4 |
| Details | DEDUCED FROM THE COORDINATION. SODIUM WAS PRESENT IN THE CRYSTALLIZATION SOLUTION. |
| Chain | Residue |
| A | ASP69 |
| A | ASP103 |
| A | HOH256 |
| A | ASN55 |
| site_id | NAB |
| Number of Residues | 4 |
| Details | DEDUCED FROM THE COORDINATION. SODIUM WAS PRESENT IN THE CRYSTALLIZATION SOLUTION. |
| Chain | Residue |
| B | ASN55 |
| B | ASP69 |
| B | ASP103 |
| B | HOH253 |
| site_id | ZNA |
| Number of Residues | 4 |
| Details | ONLY THE ZN1 SITE OF THE BINUCLEAR ZINC CENTER IS OCCUPIED. |
| Chain | Residue |
| A | HIS99 |
| A | HIS101 |
| A | HIS162 |
| A | HOH250 |
| site_id | ZNB |
| Number of Residues | 4 |
| Details | ONLY THE ZN1 SITE OF THE BINUCLEAR ZINC CENTER IS OCCUPIED. |
| Chain | Residue |
| B | HIS99 |
| B | HIS101 |
| B | HIS162 |
| B | HOH250 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IpNHwHGDciGGlgylqkk.G |
| Chain | Residue | Details |
| A | ILE96-GLY115 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10210203","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12019104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9416622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578564","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761816","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12019104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9416622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578564","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761816","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12019104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9545432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578564","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP103 | |
| A | ASN193 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP103 | |
| B | ASN193 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP103 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP103 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 15 |
| Chain | Residue | Details |
| A | HIS99 | metal ligand |
| A | HIS101 | metal ligand |
| A | ASP103 | metal ligand |
| A | HIS162 | metal ligand |
| A | SER181 | metal ligand |
| A | LYS184 | electrostatic stabiliser, steric role |
| A | ASN193 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS223 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 15 |
| Chain | Residue | Details |
| B | HIS99 | metal ligand |
| B | HIS101 | metal ligand |
| B | ASP103 | metal ligand |
| B | HIS162 | metal ligand |
| B | SER181 | metal ligand |
| B | LYS184 | electrostatic stabiliser, steric role |
| B | ASN193 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS223 | metal ligand |
