6FFW
Phosphotriesterase PTE_A53_5
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 | 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 | D6K404 |
| 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 | D6K404 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 403 |
| Chain | Residue |
| A | HIS201 |
| A | HIS230 |
| A | FMT401 |
| A | D6K404 |
| A | HOH501 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue D6K A 404 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | TRP131 |
| A | ASP301 |
| A | PHE306 |
| A | FMT401 |
| A | ZN402 |
| A | ZN403 |
| A | TRS405 |
| A | HOH501 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue TRS A 405 |
| Chain | Residue |
| A | ASP233 |
| A | HIS257 |
| A | LEU271 |
| A | D6K404 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | GLU181 |
| A | ARG185 |
| A | ILE215 |
| A | EDO407 |
| A | HOH511 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | GLU181 |
| A | LEU182 |
| A | ARG185 |
| A | EDO406 |
| A | HOH548 |
| A | HOH732 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1001 |
| Chain | Residue |
| B | ALA77 |
| B | VAL80 |
| B | GLU115 |
| B | HOH1123 |
| B | HOH1337 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 1002 |
| Chain | Residue |
| B | PRO342 |
| B | THR345 |
| B | HOH1211 |
| B | HOH1238 |
| B | HOH1296 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 1004 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | ASP301 |
| B | FMT1003 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 1005 |
| Chain | Residue |
| B | HIS201 |
| B | HIS230 |
| B | FMT1003 |
| B | HOH1323 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide FMT B 1003 and LYS B 169 |
| Chain | Residue |
| B | HIS55 |
| B | HIS57 |
| B | VAL101 |
| B | THR103 |
| B | THR128 |
| B | GLY129 |
| B | LEU130 |
| B | ILE168 |
| B | VAL170 |
| B | THR199 |
| B | HIS201 |
| B | HIS230 |
| B | ZN1004 |
| B | ZN1005 |
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 | LYS169 | |
| B | LYS169 |
| 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 | LYS169 | |
| B | LYS169 |
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 |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 159 |
| Chain | Residue | Details |
| B | HIS55 | metal ligand |
| B | HIS57 | metal ligand |
| B | LYS169 | 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 |
