2VC5
Structural basis for natural lactonase and promiscuous phosphotriesterase activities
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 FE A1315 |
| Chain | Residue |
| A | HIS22 |
| A | HIS24 |
| A | KCX137 |
| A | ASP256 |
| A | CO1316 |
| A | HOH2064 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A1316 |
| Chain | Residue |
| A | ARG223 |
| A | FE21315 |
| A | HOH2064 |
| A | KCX137 |
| A | HIS170 |
| A | HIS199 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B1315 |
| Chain | Residue |
| B | HIS22 |
| B | HIS24 |
| B | KCX137 |
| B | ASP256 |
| B | CO1316 |
| B | HOH2062 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B1316 |
| Chain | Residue |
| B | KCX137 |
| B | HIS170 |
| B | HIS199 |
| B | ARG223 |
| B | FE21315 |
| B | HOH2062 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C1315 |
| Chain | Residue |
| C | HIS22 |
| C | HIS24 |
| C | KCX137 |
| C | ASP256 |
| C | CO1316 |
| C | HOH2056 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO C1316 |
| Chain | Residue |
| C | KCX137 |
| C | HIS170 |
| C | HIS199 |
| C | ARG223 |
| C | FE21315 |
| C | HOH2013 |
| C | HOH2056 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D1315 |
| Chain | Residue |
| D | HIS22 |
| D | HIS24 |
| D | KCX137 |
| D | ASP256 |
| D | CO1316 |
| D | HOH2061 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO D1316 |
| Chain | Residue |
| D | KCX137 |
| D | HIS170 |
| D | HIS199 |
| D | ARG223 |
| D | FE21315 |
| D | HOH2061 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1317 |
| Chain | Residue |
| A | TYR99 |
| A | ILE100 |
| A | ASP101 |
| B | PHE104 |
| B | EDO1321 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D1317 |
| Chain | Residue |
| D | ASN172 |
| D | ALA173 |
| D | HIS174 |
| D | ASP202 |
| D | PHE229 |
| D | HOH2045 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C1317 |
| Chain | Residue |
| C | ASN160 |
| C | LYS164 |
| C | GLY189 |
| C | ASP191 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D1318 |
| Chain | Residue |
| C | PHE104 |
| D | TYR99 |
| D | ILE100 |
| D | ASP101 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B1317 |
| Chain | Residue |
| B | TYR257 |
| B | CYS258 |
| B | ILE261 |
| B | ALA266 |
| B | LYS271 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A1318 |
| Chain | Residue |
| A | ASN160 |
| A | LYS164 |
| A | GLY189 |
| A | ASP191 |
| A | LYS194 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B1318 |
| Chain | Residue |
| B | ASN160 |
| B | LYS164 |
| B | GLY189 |
| B | VAL190 |
| B | ASP191 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D1319 |
| Chain | Residue |
| D | ASN160 |
| D | LYS164 |
| D | GLY189 |
| D | VAL190 |
| D | ASP191 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B1319 |
| Chain | Residue |
| B | SER171 |
| B | ASN172 |
| B | ALA173 |
| B | ASP202 |
| B | ARG223 |
| B | PHE229 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B1320 |
| Chain | Residue |
| B | EDO1321 |
| A | PHE104 |
| B | ILE98 |
| B | TYR99 |
| B | ILE100 |
| B | ASP101 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A1319 |
| Chain | Residue |
| A | LYS14 |
| A | GLY17 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D1320 |
| Chain | Residue |
| D | GLY128 |
| D | THR129 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1320 |
| Chain | Residue |
| A | LEU5 |
| A | ASP9 |
| A | SER10 |
| A | ASN131 |
| A | LYS132 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1321 |
| Chain | Residue |
| A | EDO1317 |
| B | ASP101 |
| B | LEU102 |
| B | PHE104 |
| B | GOL1320 |
| B | EDO1323 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C1318 |
| Chain | Residue |
| C | LEU39 |
| C | ILE261 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B1322 |
| Chain | Residue |
| B | ALA266 |
| B | TRP278 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B1323 |
| Chain | Residue |
| B | LEU102 |
| B | PRO103 |
| B | LEU107 |
| B | ASP148 |
| B | EDO1321 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A1321 |
| Chain | Residue |
| A | ASP141 |
| A | SER171 |
| A | ASN172 |
| A | ALA173 |
| A | ASP202 |
| A | ARG223 |
| A | PHE229 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C1319 |
| Chain | Residue |
| C | TYR99 |
| C | ILE100 |
| C | ASP101 |
| D | PHE104 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1324 |
| Chain | Residue |
| A | SER29 |
| A | GLY71 |
| B | PRO103 |
| B | PHE104 |
| site_id | DC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D1321 |
| Chain | Residue |
| D | ALA266 |
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 |
| A | HIS22 | |
| B | ASP256 | |
| C | HIS22 | |
| C | HIS24 | |
| C | HIS170 | |
| C | HIS199 | |
| C | ASP256 | |
| D | HIS22 | |
| D | HIS24 | |
| D | HIS170 | |
| D | HIS199 | |
| A | HIS24 | |
| D | ASP256 | |
| A | HIS170 | |
| A | HIS199 | |
| A | ASP256 | |
| B | HIS22 | |
| B | HIS24 | |
| B | HIS170 | |
| B | HIS199 |
| 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 |
| A | KCX137 | |
| B | KCX137 | |
| C | KCX137 | |
| D | KCX137 |
