1P6C
crystal structure of phosphotriesterase triple mutant H254G/H257W/L303T complexed with diisopropylmethylphosphonate
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 | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | DII7 |
| A | HIS55 |
| A | HIS57 |
| A | KCX169 |
| A | ASP301 |
| A | ZN402 |
| A | HOH456 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | HIS201 |
| A | HIS230 |
| A | ZN401 |
| A | HOH456 |
| A | DII7 |
| A | KCX169 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 403 |
| Chain | Residue |
| B | HOH16 |
| B | HIS55 |
| B | HIS57 |
| B | KCX169 |
| B | ASP301 |
| B | ZN404 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 404 |
| Chain | Residue |
| B | DII8 |
| B | HOH16 |
| B | KCX169 |
| B | HIS201 |
| B | HIS230 |
| B | ZN403 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EBP A 5 |
| Chain | Residue |
| A | GLN155 |
| A | TYR156 |
| B | PHE51 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EBP B 6 |
| Chain | Residue |
| A | PHE51 |
| A | GLU71 |
| B | GLN155 |
| B | TYR156 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DII A 7 |
| Chain | Residue |
| A | HIS57 |
| A | TRP131 |
| A | KCX169 |
| A | HIS201 |
| A | ASP301 |
| A | ZN401 |
| A | ZN402 |
| A | HOH456 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DII B 8 |
| Chain | Residue |
| B | TRP131 |
| B | HIS201 |
| B | ZN404 |
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 site: {"evidences":[{"source":"PubMed","id":"15369336","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P6C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"15369336","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P6C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15369336","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P6C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez2 |
| Chain | Residue | Details |
| A | GLY254 | |
| A | ASP233 | |
| A | ASP301 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ez2 |
| Chain | Residue | Details |
| B | GLY254 | |
| B | ASP233 | |
| B | ASP301 |
