2UYX
metallo-beta-lactamase (1BC2) single point mutant D120S
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A1292 |
| Chain | Residue |
| A | HIS118 |
| A | HOH2280 |
| A | HOH2281 |
| A | SER120 |
| A | HIS196 |
| A | GOL1293 |
| A | ZN1296 |
| A | ZN1297 |
| A | HOH2277 |
| A | HOH2278 |
| A | HOH2279 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A1293 |
| Chain | Residue |
| A | HIS118 |
| A | ALA119 |
| A | SER120 |
| A | CYS221 |
| A | GOL1292 |
| A | ZN1296 |
| A | ZN1297 |
| A | HOH2277 |
| A | HOH2279 |
| A | HOH2280 |
| A | HOH2281 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A1294 |
| Chain | Residue |
| A | ALA117 |
| A | HIS118 |
| A | ASN149 |
| A | THR197 |
| A | ASP199 |
| A | ASP236 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A1295 |
| Chain | Residue |
| A | GLU97 |
| A | GLU130 |
| A | ARG131 |
| A | HOH2077 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A1296 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | GOL1292 |
| A | GOL1293 |
| A | HOH2281 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A1297 |
| Chain | Residue |
| A | CYS221 |
| A | HIS263 |
| A | GOL1292 |
| A | GOL1293 |
| A | HOH2280 |
| A | HOH2283 |
Functional Information from PROSITE/UniProt
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7588620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qh5 |
| Chain | Residue | Details |
| A | SER120 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| A | HIS116 | metal ligand |
| A | HIS118 | metal ligand |
| A | SER120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS196 | metal ligand |
| A | ASN233 | electrostatic stabiliser, hydrogen bond donor |






