The enzyme catalyzes the stereospecific hydroxylation of the glycine alpha-carbon of all the peptidylglycine substrates. It binds two copper ions largely separated in space (PMID10580705).
DETAILS ON METAL
CU 357 x |
|
| This copper is conventionally called CuH (or CuA). It provides an additional electron through long-range electron transfer (PMID15080705). |
| Site type | Physiological Metal |
| mononuclear | copper |
| Metal in the Resting State | |||
| Oxidation State |
Coordination Geometry | Coordination Number | PDB |
| 2 | tShaped | 3 | 1phm |
| Metal in the reaction stages | ||||||
| Step | Metal function(s) | Initial-Final Oxid. states | Initial-Final Geometry | Initial-Final Coord. # | Initial PDB | Final PDB |
| Step 1 | Not active |
+2 - +2 |
tShaped - tShaped |
3 - 3 | - | - |
| Step 2 | One electron acceptor |
+2 - +1 |
tShaped - tShaped |
3 - 3 | - | - |
| Step 3 | Not active |
+1 - +1 |
tShaped - tShaped |
3 - 3 | 1sdw | - |
| Step 4 | Not active |
+1 - +1 |
tShaped - tShaped |
3 - 3 | - | - |
| Step 5 | Not active |
+1 - +1 |
tShaped - tShaped |
3 - 3 | - | - |
| Step 6 | One electron donor |
+1 - +2 |
tShaped - tShaped |
3 - 3 | - | - |
| Step 7 | Not present |
+2 - +2 |
tShaped - tShaped |
3 - 3 | - | - |
* N.B. There may be steps that are not described in between two annotated steps. Consequently the product species of step n may differ from the reagent species of step n+1.