6AML
Phosphotriesterase variant S8
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 |
| G | 0004063 | molecular_function | aryldialkylphosphatase activity |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0008270 | molecular_function | zinc ion binding |
| G | 0009056 | biological_process | catabolic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| G | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 2401 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | KCX169 |
| A | ASP301 |
| A | CAC2403 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 2402 |
| Chain | Residue |
| A | KCX169 |
| A | HIS201 |
| A | HIS230 |
| A | CAC2403 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue CAC A 2403 |
| Chain | Residue |
| A | HIS55 |
| A | HIS57 |
| A | TRP131 |
| A | KCX169 |
| A | HIS201 |
| A | HIS230 |
| A | ASP301 |
| A | ZN2401 |
| A | ZN2402 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue MPD A 2404 |
| Chain | Residue |
| A | GLU81 |
| A | VAL84 |
| A | ARG88 |
| A | GLU115 |
| A | ALA119 |
| A | ARG246 |
| A | HOH2515 |
| A | HOH2527 |
| A | HOH2601 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 2405 |
| Chain | Residue |
| A | PHE72 |
| A | HOH2539 |
| G | GLU145 |
| G | GLN148 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue MPD A 2406 |
| Chain | Residue |
| A | GLY291 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MPD A 2407 |
| Chain | Residue |
| A | PHE51 |
| A | GLN343 |
| A | THR350 |
| A | VAL351 |
| A | HOH2674 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN G 2401 |
| Chain | Residue |
| G | HIS55 |
| G | HIS57 |
| G | KCX169 |
| G | ASP301 |
| G | CAC2403 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN G 2402 |
| Chain | Residue |
| G | KCX169 |
| G | HIS201 |
| G | HIS230 |
| G | CAC2403 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue CAC G 2403 |
| Chain | Residue |
| G | HIS55 |
| G | HIS57 |
| G | TRP131 |
| G | KCX169 |
| G | HIS201 |
| G | HIS230 |
| G | ASP301 |
| G | ZN2401 |
| G | ZN2402 |
| G | MPD2405 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MPD G 2404 |
| Chain | Residue |
| G | LYS77 |
| G | GLU81 |
| G | VAL84 |
| G | GLU115 |
| G | HOH2513 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MPD G 2405 |
| Chain | Residue |
| G | SER308 |
| G | TYR309 |
| G | CAC2403 |
| G | HOH2524 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue MPD G 2406 |
| Chain | Residue |
| G | PHE51 |
| G | ARG337 |
| G | GLN343 |
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 | ASP301 | |
| G | HIS55 | |
| G | HIS57 | |
| G | HIS201 | |
| G | HIS230 | |
| G | ASP301 | |
| A | HIS55 | |
| A | HIS57 | |
| A | HIS201 | |
| A | 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 | |
| G | 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 | |
| G | KCX169 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 159 |
| Chain | Residue | Details |
| A | HIS57 | metal ligand |
| A | KCX169 | metal ligand |
| A | HIS55 | metal ligand |
| A | HIS201 | metal ligand |
| A | HIS230 | metal ligand |
| A | ALA233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER254 | 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 |
| G | HIS55 | metal ligand |
| G | HIS57 | metal ligand |
| G | KCX169 | metal ligand |
| G | HIS201 | metal ligand |
| G | HIS230 | metal ligand |
| G | ALA233 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | SER254 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| G | ASP301 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
