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 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
| Chain | Residue | Details |
| A | HIS55 | |
| B | ASP301 | |
| A | HIS57 | |
| A | HIS201 | |
| A | HIS230 | |
| A | ASP301 | |
| B | HIS55 | |
| B | HIS57 | |
| B | HIS201 | |
| B | HIS230 | |
| Chain | Residue | Details |
| A | KCX169 | |
| B | KCX169 | |
| Chain | Residue | Details |
| A | KCX169 | |
| B | KCX169 | |
