4KEV
Crystal structure of SsoPox W263L
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004063 | molecular_function | aryldialkylphosphatase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009056 | biological_process | catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004063 | molecular_function | aryldialkylphosphatase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009056 | biological_process | catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004063 | molecular_function | aryldialkylphosphatase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009056 | biological_process | catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004063 | molecular_function | aryldialkylphosphatase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009056 | biological_process | catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 401 |
| Chain | Residue |
| A | HIS22 |
| A | HIS24 |
| A | KCX137 |
| A | ASP256 |
| A | HOH551 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 402 |
| Chain | Residue |
| A | HOH551 |
| A | KCX137 |
| A | HIS170 |
| A | HIS199 |
| A | ARG223 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 B 401 |
| Chain | Residue |
| B | HIS22 |
| B | HIS24 |
| B | KCX137 |
| B | ASP256 |
| B | CO402 |
| B | HOH549 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 402 |
| Chain | Residue |
| B | KCX137 |
| B | HIS170 |
| B | HIS199 |
| B | ARG223 |
| B | FE2401 |
| B | HOH549 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 C 401 |
| Chain | Residue |
| C | HIS22 |
| C | HIS24 |
| C | KCX137 |
| C | ASP256 |
| C | CO402 |
| C | HOH527 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO C 402 |
| Chain | Residue |
| C | KCX137 |
| C | HIS170 |
| C | HIS199 |
| C | FE2401 |
| C | HOH527 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 D 401 |
| Chain | Residue |
| D | HIS22 |
| D | HIS24 |
| D | KCX137 |
| D | ASP256 |
| D | CO402 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO D 402 |
| Chain | Residue |
| D | KCX137 |
| D | HIS170 |
| D | HIS199 |
| D | ARG223 |
| D | FE2401 |
Functional Information from PROSITE/UniProt
| site_id | PS01322 |
| Number of Residues | 9 |
| Details | PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLiHEHL |
| Chain | Residue | Details |
| A | GLY17-LEU25 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
