3F9O
Crystal Structure of the Di-Zinc Carbapenemase CphA from Aeromonas Hydrophila
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | HOH107 |
| A | HIS118 |
| A | ASP120 |
| A | HIS196 |
| A | HIS263 |
| A | ZN308 |
| A | ZN309 |
| A | HOH334 |
| A | HOH474 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | HIS176 |
| A | ASP177 |
| A | HOH465 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | ALA237 |
| A | ASP238 |
| A | VAL239 |
| A | LYS240 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | SER104 |
| A | LYS106 |
| A | HOH348 |
| A | HOH466 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 A 5 |
| Chain | Residue |
| A | LEU249 |
| A | LYS250 |
| A | LYS253 |
| A | LEU254 |
| A | ILE256 |
| A | HOH365 |
| A | HOH421 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO3 A 6 |
| Chain | Residue |
| A | ARG158 |
| A | ASP166 |
| A | HOH449 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 7 |
| Chain | Residue |
| A | HOH19 |
| A | ASN116 |
| A | ASN220 |
| A | CYS221 |
| A | ILE222 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 9 |
| Chain | Residue |
| A | GLN47 |
| A | HOH393 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 10 |
| Chain | Residue |
| A | CL11 |
| A | ZN310 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 11 |
| Chain | Residue |
| A | CL10 |
| A | HIS289 |
| A | LEU293 |
| A | ZN310 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 12 |
| Chain | Residue |
| A | HIS289 |
| A | GLY290 |
| A | ZN310 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 308 |
| Chain | Residue |
| A | SO41 |
| A | ASP120 |
| A | CYS221 |
| A | HIS263 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 309 |
| Chain | Residue |
| A | SO41 |
| A | HIS118 |
| A | HIS196 |
| A | HOH474 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 310 |
| Chain | Residue |
| A | CL10 |
| A | CL11 |
| A | CL12 |
| A | HIS289 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15588826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17307979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18563261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19651913","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20527888","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15588826","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15588826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18563261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20527888","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15588826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17307979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20527888","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15588826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17307979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18563261","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 | ASP120 | |
| A | ASN233 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP120 |






