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).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 422 A | MG | magnesium | magnesium/manganese | mononuclear | Coordinates substrate Electrostatic stabiliser Increases electrophilicity |
*It refers to the MACiE reference pdb: 13pk
| Metal/s Properties in Resting State | ||||||
| MG 422 A | Resting state enzyme (2ie8) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | 0 | |||||
| Notes | - | |||||
| References |
| -Flachner B, Kovári Z, Varga A, Gugolya Z, Vonderviszt F, Náray-Szabó G, Vas M Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. Biochemistry. 2004 Mar 30;43(12):3436-49.(MEDLINE:15035615) |