1QW7
Structure of an Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds
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 | 7 |
| Details | BINDING SITE FOR RESIDUE CO A 601 |
| Chain | Residue |
| A | KCX169 |
| A | HIS201 |
| A | HIS230 |
| A | ARG254 |
| A | CO602 |
| A | HOH802 |
| A | HOH826 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 602 |
| Chain | Residue |
| A | KCX169 |
| A | ASP301 |
| A | CO601 |
| A | HOH802 |
| A | HIS55 |
| A | HIS57 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 603 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | KCX169 |
| B | ASP301 |
| B | CO604 |
| B | HOH774 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO B 604 |
| Chain | Residue |
| B | KCX169 |
| B | HIS201 |
| B | HIS230 |
| B | ARG254 |
| B | CO603 |
| B | HOH774 |
| B | HOH776 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 605 |
| Chain | Residue |
| A | ASN38 |
| A | ILE154 |
| A | HOH913 |
| B | HOH719 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 606 |
| Chain | Residue |
| B | ASN38 |
| B | ILE154 |
| B | HOH802 |
| B | HOH830 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EBP B 701 |
| Chain | Residue |
| A | GLN155 |
| A | TYR156 |
| B | GLU71 |
| B | THR350 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EBP A 702 |
| Chain | Residue |
| A | PHE51 |
| A | GLU71 |
| A | HOH969 |
| B | GLN155 |
| B | TYR156 |
| B | ARG164 |
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 | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez2 |
| Chain | Residue | Details |
| A | ARG254 | |
| A | ASP233 | |
| A | ASP301 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez2 |
| Chain | Residue | Details |
| B | ARG254 | |
| B | ASP233 | |
| B | ASP301 |
| 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 | SER205 | metal ligand |
| A | THR234 | metal ligand |
| A | LEU237 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER258 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | GLY305 | 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 | SER205 | metal ligand |
| B | THR234 | metal ligand |
| B | LEU237 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | SER258 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | GLY305 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
