3URQ
Crystal Structure of PTE mutant H254G/H257W/L303T/M317L/I106C/F132I/L271I/K185R/I274N/A80V/R67H with cyclohexyl methylphosphonate inhibitor
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 | 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 | 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 | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 801 |
| Chain | Residue |
| A | KCX169 |
| A | HIS201 |
| A | HIS230 |
| A | QMP902 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 802 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | KCX169 |
| A | ASP301 |
| A | QMP902 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE QMP A 902 |
| Chain | Residue |
| A | GLY60 |
| A | TRP131 |
| A | KCX169 |
| A | HIS201 |
| A | HIS230 |
| A | ASP301 |
| A | THR303 |
| A | PHE306 |
| A | CO801 |
| A | CO802 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD A 903 |
| Chain | Residue |
| A | GLY174 |
| A | LYS175 |
| A | GLN206 |
| A | ASP208 |
| A | GLN211 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD A 904 |
| Chain | Residue |
| A | HIS230 |
| A | ASP233 |
| A | ASP253 |
| A | GLY254 |
| A | ARG280 |
| A | ASP301 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD A 906 |
| Chain | Residue |
| A | ASP133 |
| A | PRO134 |
| A | PRO135 |
| B | ASP133 |
| B | PRO134 |
| B | PRO135 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 803 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | KCX169 |
| B | ASP301 |
| B | QMP901 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 804 |
| Chain | Residue |
| B | KCX169 |
| B | HIS201 |
| B | HIS230 |
| B | QMP901 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE QMP B 901 |
| Chain | Residue |
| B | GLY60 |
| B | TRP131 |
| B | KCX169 |
| B | HIS201 |
| B | HIS230 |
| B | ASP301 |
| B | THR303 |
| B | PHE306 |
| B | CO803 |
| B | CO804 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD B 905 |
| Chain | Residue |
| B | HIS230 |
| B | ASP232 |
| B | ASP233 |
| B | ASP253 |
| B | GLY254 |
| 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 |
