The enzyme catalyzes the reduction of arsenate (HAsO) to arsenite (H3AsO3) and participates in the arsenic detoxification systems of prokaryotes and eukaryotes PMID12072565. The enzyme from Staphylococcus aureus binds a potassium ion that is involved in stabilizing the structure of the active site and increases the activity of the enzyme PMID16797027.
K 133 _ IN THE RESTING STATE ENZYME
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Representative PDB structure for K 133 _ in the resting state enzyme | |
|   | ||
| PDB code | 1ljl | |
| Metal Type in the PDB | potassium | |
| Residue name of the metal in the PDB | K | |
| Residue number of the metal in the PDB | 133 | |
| Chain of the metal in the PDB | _ | |
| Atom name of the metal in the PDB | K | |
| Download the coordinates file of the metal site | NOTES ON PDB: | |
| First Coordination Sphere | ||||||
| Ligand Type | Ligand Identity | Residue In MACiE | Donors | Bind Mode | Catalytic? | Notes |
| residue | ASN 13 A | ASN 13 A | OD1 | monodentate | Yes | It is involved in the hydrogen bond network and behaves as an electrostatic stabilizer. |
| residue | SER 36 A | SER 36 A | O,OG | bidentate | No | - |
| residue | THR 63 A | THR 63 A | O | monodentate | No | - |
| residue | ASP 65 A | ASP 65 A | OD2 | monodentate | No | - |
| water | HOH 136 _ | - | O | monodentate | No | - |
| water | HOH 143 _ | - | O | monodentate | No | - |








