4KEZ
Crystal structure of SsoPox W263F
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 | HOH773 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 402 |
| Chain | Residue |
| A | FE2401 |
| A | HOH773 |
| A | KCX137 |
| A | HIS170 |
| A | HIS199 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | ASN160 |
| A | LYS164 |
| A | GLY189 |
| A | VAL190 |
| A | ASP191 |
| A | LYS194 |
| A | HOH639 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASN172 |
| A | ALA173 |
| A | HIS174 |
| A | ASP202 |
| A | PHE229 |
| A | HOH535 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | PRO4 |
| A | LEU5 |
| A | LYS8 |
| A | ASP9 |
| A | SER10 |
| A | LEU130 |
| A | ASN131 |
| A | LYS132 |
| A | HOH533 |
| A | HOH660 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 406 |
| Chain | Residue |
| A | LEU102 |
| A | PRO103 |
| A | PHE106 |
| A | LEU107 |
| A | ASP148 |
| A | LYS151 |
| A | HOH648 |
| A | HOH679 |
| site_id | AC7 |
| 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 | HOH755 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 402 |
| Chain | Residue |
| B | KCX137 |
| B | HIS170 |
| B | HIS199 |
| B | FE2401 |
| B | HOH755 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | ASN160 |
| B | LYS164 |
| B | GLY189 |
| B | VAL190 |
| B | ASP191 |
| B | LYS194 |
| B | HOH617 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | SER171 |
| B | ASN172 |
| B | ALA173 |
| B | HIS174 |
| B | ASP202 |
| B | PHE229 |
| B | HOH582 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| B | PRO4 |
| B | LEU5 |
| B | LYS8 |
| B | ASP9 |
| B | SER10 |
| B | ASN131 |
| B | LYS132 |
| B | HOH565 |
| site_id | BC3 |
| 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 | HOH753 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO C 402 |
| Chain | Residue |
| C | KCX137 |
| C | HIS170 |
| C | HIS199 |
| C | FE2401 |
| C | EDO405 |
| C | HOH753 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| C | ASN160 |
| C | LYS164 |
| C | GLY189 |
| C | VAL190 |
| C | ASP191 |
| C | HOH589 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 404 |
| Chain | Residue |
| C | HOH547 |
| C | HOH578 |
| C | SER171 |
| C | ASN172 |
| C | ALA173 |
| C | HIS174 |
| C | ASP202 |
| C | PHE229 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 405 |
| Chain | Residue |
| C | TYR97 |
| C | HIS170 |
| C | ARG223 |
| C | CO402 |
| C | HOH663 |
| C | HOH753 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 406 |
| Chain | Residue |
| C | ASP214 |
| C | GLY246 |
| C | TYR247 |
| C | ASP249 |
| C | LYS250 |
| C | HOH677 |
| site_id | BC9 |
| 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 | HOH759 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO D 402 |
| Chain | Residue |
| D | KCX137 |
| D | HIS170 |
| D | HIS199 |
| D | FE2401 |
| D | HOH759 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 403 |
| Chain | Residue |
| D | ASN160 |
| D | LYS164 |
| D | GLY189 |
| D | ASP191 |
| D | LYS194 |
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: BINDING => ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1 |
| Chain | Residue | Details |
| B | HIS199 | |
| B | ASP256 | |
| C | HIS22 | |
| C | HIS24 | |
| C | HIS170 | |
| C | HIS199 | |
| C | ASP256 | |
| D | HIS22 | |
| D | HIS24 | |
| D | HIS170 | |
| D | HIS199 | |
| D | ASP256 | |
| A | HIS22 | |
| A | HIS24 | |
| A | HIS170 | |
| A | HIS199 | |
| A | ASP256 | |
| B | HIS22 | |
| B | HIS24 | |
| B | HIS170 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1 |
| Chain | Residue | Details |
| A | KCX137 | |
| B | KCX137 | |
| C | KCX137 | |
| D | KCX137 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1 |
| Chain | Residue | Details |
| D | KCX137 | |
| A | KCX137 | |
| B | KCX137 | |
| C | KCX137 |
