4KER
Crystal structure of SsoPox W263V
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 | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 A 401 |
| Chain | Residue |
| A | HIS22 |
| A | HIS24 |
| A | KCX137 |
| A | ASP256 |
| A | CO402 |
| A | HOH599 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 402 |
| Chain | Residue |
| A | ARG223 |
| A | FE2401 |
| A | HOH599 |
| A | KCX137 |
| A | HIS170 |
| A | HIS199 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | SER171 |
| A | ASN172 |
| A | ALA173 |
| A | ASP202 |
| A | PHE229 |
| A | HOH544 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASN160 |
| A | LYS164 |
| A | GLY189 |
| A | ASP191 |
| A | HOH579 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | HIS120 |
| A | GLY125 |
| A | GLY128 |
| A | THR129 |
| A | LEU130 |
| C | LYS164 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 406 |
| Chain | Residue |
| A | ASP256 |
| A | CYS258 |
| A | HOH599 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 B 401 |
| Chain | Residue |
| B | HIS22 |
| B | HIS24 |
| B | KCX137 |
| B | ASP256 |
| B | CO402 |
| B | GOL406 |
| B | HOH539 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 402 |
| Chain | Residue |
| B | KCX137 |
| B | HIS170 |
| B | HIS199 |
| B | FE2401 |
| B | GOL406 |
| B | HOH539 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | LEU25 |
| B | ARG26 |
| B | ASP66 |
| B | THR68 |
| B | GLY73 |
| B | ASP75 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | ASN172 |
| B | ALA173 |
| B | ASP202 |
| B | HOH561 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| B | ASN160 |
| B | LYS164 |
| B | GLY189 |
| B | ASP191 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 406 |
| Chain | Residue |
| B | HIS24 |
| B | TYR97 |
| B | KCX137 |
| B | HIS170 |
| B | ARG223 |
| B | ASP256 |
| B | CYS258 |
| B | FE2401 |
| B | CO402 |
| B | HOH539 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 407 |
| Chain | Residue |
| B | HIS120 |
| B | GLY128 |
| B | THR129 |
| B | HOH532 |
| site_id | BC5 |
| 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 | HOH583 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO C 402 |
| Chain | Residue |
| C | KCX137 |
| C | HIS170 |
| C | HIS199 |
| C | ARG223 |
| C | FE2401 |
| C | GOL404 |
| C | HOH583 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 403 |
| Chain | Residue |
| C | SER171 |
| C | ASN172 |
| C | ALA173 |
| C | HIS174 |
| C | ASP202 |
| C | PHE229 |
| C | HOH515 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 404 |
| Chain | Residue |
| C | HOH583 |
| C | ARG223 |
| C | ASP256 |
| C | CYS258 |
| C | ILE261 |
| C | CO402 |
| C | EDO407 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 405 |
| Chain | Residue |
| A | ARG77 |
| C | ASN160 |
| C | LYS164 |
| C | GLY189 |
| C | VAL190 |
| C | ASP191 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 406 |
| Chain | Residue |
| C | HOH519 |
| C | HOH525 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 407 |
| Chain | Residue |
| C | THR265 |
| C | ALA266 |
| C | GOL404 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 D 401 |
| Chain | Residue |
| D | HIS22 |
| D | HIS24 |
| D | KCX137 |
| D | ASP256 |
| D | CO402 |
| D | HOH586 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO D 402 |
| Chain | Residue |
| D | KCX137 |
| D | HIS170 |
| D | HIS199 |
| D | FE2401 |
| D | HOH586 |
| D | HOH588 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 403 |
| Chain | Residue |
| D | SER171 |
| D | ALA173 |
| D | HIS174 |
| D | ASP202 |
| D | PHE229 |
| D | HOH507 |
| D | HOH549 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 404 |
| Chain | Residue |
| D | PRO4 |
| D | LEU5 |
| D | LYS8 |
| D | ASP9 |
| D | SER10 |
| D | LEU130 |
| D | ASN131 |
| D | LYS132 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 405 |
| Chain | Residue |
| D | ASN160 |
| D | LYS164 |
| D | GLY189 |
| D | ASP191 |
| D | LYS194 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 406 |
| Chain | Residue |
| D | GLY128 |
| D | THR129 |
| D | HOH508 |
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 |






