6FWE
Phosphotriesterase PTE_C23_6
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue FMT A 401 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | TRP131 |
| A | LYS169 |
| A | HIS201 |
| A | HIS230 |
| A | ZN402 |
| A | ZN403 |
| A | E9E404 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | ASP301 |
| A | FMT401 |
| A | E9E404 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 403 |
| Chain | Residue |
| A | HIS201 |
| A | HIS230 |
| A | FMT401 |
| A | E9E404 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue E9E A 404 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | TRP131 |
| A | HIS201 |
| A | HIS230 |
| A | ASP301 |
| A | FMT401 |
| A | ZN402 |
| A | ZN403 |
| A | HOH715 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue E8N A 405 |
| Chain | Residue |
| A | GLU144 |
| A | VAL341 |
| A | SER342 |
| A | THR345 |
| A | HOH707 |
| A | HOH734 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | TYR156 |
| A | GLY157 |
| A | GLU159 |
| A | ASP160 |
| A | THR161 |
| A | GLY162 |
| A | HOH579 |
| A | HOH688 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | ALA63 |
| A | GLY64 |
| A | ARG67 |
| A | GLY107 |
| A | ARG108 |
| A | GLU159 |
| A | HOH555 |
| A | HOH577 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 408 |
| Chain | Residue |
| A | SER205 |
| A | THR234 |
| A | ASP235 |
| A | ASP236 |
| A | HOH503 |
| A | HOH506 |
| A | HOH659 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 409 |
| Chain | Residue |
| A | TRP277 |
| A | GLN278 |
| A | ARG331 |
| A | HOH527 |
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 | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7794910","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EZ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O4Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 | LYS169 | 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 |






