The enzyme catalyzes the hydrolysis of beta-aspartyl dipeptides. It binds two divalent metal ions in a dinuclear site (PMID15882050).
ZN 800 x IN THE RESTING STATE ENZYME
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Representative PDB structure for ZN 800 x in the resting state enzyme | |
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| PDB code | 1onw | |
| Metal Type in the PDB | zinc | |
| Residue name of the metal in the PDB | ZN | |
| Residue number of the metal in the PDB | 800 | |
| Chain of the metal in the PDB | _ | |
| Atom name of the metal in the PDB | ZN | |
| 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 | HIS 68 A | HIS 68 A | NE2 | monodentate | No | - |
| residue | HIS 70 A | HIS 70 A | NE2 | monodentate | No | - |
| residue | KCX 162 A | KCX 162 A | OX2 | monodentate | No | This species is a carboxylated lysine. |
| residue | ASP 285 A | ASP 285 A | OD1 | monodentate | Yes | Asp285 is involved in proton relay. |
| water | HOH 92 _ | - | O | monodentate | No | - |






