3UR2
Crystal Structure of PTE mutant H254G/H257W/L303T/K185R/I274N/A80V
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004063 | molecular_function | aryldialkylphosphatase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009056 | biological_process | catabolic process |
| A | 0016020 | cellular_component | membrane |
| 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 | 0005886 | cellular_component | plasma membrane |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009056 | biological_process | catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 801 |
| Chain | Residue |
| A | KCX169 |
| A | HIS201 |
| A | HIS230 |
| A | HOH1189 |
| A | HOH1190 |
| A | HOH1244 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 802 |
| Chain | Residue |
| A | ASP301 |
| A | HOH1244 |
| A | HIS55 |
| A | HIS57 |
| A | KCX169 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD A 900 |
| Chain | Residue |
| A | HIS230 |
| A | ASP232 |
| A | ASP233 |
| A | ASP253 |
| A | GLY254 |
| A | TRP257 |
| A | ARG280 |
| A | ASP301 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD A 902 |
| Chain | Residue |
| A | SER308 |
| A | HOH1151 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 903 |
| Chain | Residue |
| A | ALA63 |
| A | GLY64 |
| A | LEU66 |
| A | ARG67 |
| A | GLY107 |
| A | ARG108 |
| A | ASP109 |
| A | HOH1058 |
| A | HOH1121 |
| A | HOH1210 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 904 |
| Chain | Residue |
| A | ARG89 |
| A | PHE304 |
| A | PRO322 |
| A | ASP323 |
| A | GLY324 |
| A | HOH1039 |
| A | HOH1076 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 905 |
| Chain | Residue |
| A | ARG76 |
| A | LYS77 |
| A | GLU115 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 906 |
| Chain | Residue |
| A | SER111 |
| A | ALA114 |
| A | ARG118 |
| A | ILE163 |
| A | SER238 |
| A | HOH1254 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 803 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | KCX169 |
| B | ASP301 |
| B | HOH1245 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 804 |
| Chain | Residue |
| B | KCX169 |
| B | HIS201 |
| B | HIS230 |
| B | HOH1245 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD B 901 |
| Chain | Residue |
| B | HIS230 |
| B | ASP232 |
| B | ASP233 |
| B | ASP253 |
| B | GLY254 |
| B | TRP257 |
| B | ARG280 |
| B | ASP301 |
Functional Information from PROSITE/UniProt
| site_id | PS01322 |
| Number of Residues | 9 |
| Details | PHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLtHEHI |
| Chain | Residue | Details |
| A | GLY50-ILE58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL |
| Chain | Residue | Details |
| A | HIS55 | |
| B | ASP301 | |
| A | HIS57 | |
| A | HIS201 | |
| A | HIS230 | |
| A | ASP301 | |
| B | HIS55 | |
| B | HIS57 | |
| B | HIS201 | |
| B | HIS230 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL |
| Chain | Residue | Details |
| A | KCX169 | |
| B | KCX169 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL |
| Chain | Residue | Details |
| A | KCX169 | |
| B | KCX169 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 159 |
| Chain | Residue | Details |
| A | HIS55 | metal ligand |
| A | HIS57 | metal ligand |
| A | KCX169 | metal ligand |
| A | HIS201 | metal ligand |
| A | HIS230 | metal ligand |
| A | ASP233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 159 |
| Chain | Residue | Details |
| B | HIS55 | metal ligand |
| B | HIS57 | metal ligand |
| B | KCX169 | metal ligand |
| B | HIS201 | metal ligand |
| B | HIS230 | metal ligand |
| B | ASP233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
