The enzyme catalyzes the transfer of a phosphoryl group from 1,3-bis-phosphoglycerate to ADP to form 3-phosphoglycerate and ATP in the presence of magnesium. It is a monomeric enzyme comprised of globular N- and C-terminal domains. The active site is located at the interface between the two domains (PMID17045964).
MG 422 A IN THE RESTING STATE ENZYME
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Representative PDB structure for MG 422 A in the resting state enzyme | |
| PDB code | 2ie8 | |
| Metal Type in the PDB | none | |
| Residue name of the metal in the PDB | none | |
| Residue number of the metal in the PDB | 0 | |
| Chain of the metal in the PDB | none | |
| Atom name of the metal in the PDB | none | |
| 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 |