Glycerate kinase
From Proteopedia
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[[Image:1to6.png|left|200px|thumb|Crystal Structure of glycerate kinase, [[1to6]]]] | [[Image:1to6.png|left|200px|thumb|Crystal Structure of glycerate kinase, [[1to6]]]] | ||
{{STRUCTURE_1to6| PDB=1to6 | SIZE=400| SCENE=Glycerate_kinase/Glycerate_kinase/1|right|CAPTION=Glycerate kinase dimer complex with SO4 ions, [[1to6]] }} | {{STRUCTURE_1to6| PDB=1to6 | SIZE=400| SCENE=Glycerate_kinase/Glycerate_kinase/1|right|CAPTION=Glycerate kinase dimer complex with SO4 ions, [[1to6]] }} | ||
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Revision as of 08:07, 4 November 2012
Image:1to6.png
Crystal Structure of glycerate kinase, 1to6
Glycerate kinase (GK) catalyzes the conversion of ATP + glycerate to ADP + 3-phospho-glycerate. GK participates in the metabolic pathways of serine/glycine/threonine, glycolipid and glyoxylate-dicarboxylate. GK is the last step in the pathway which starts with glucose and ends with 2-phosphoglycerate.
Contents |
3D Structures of glycerate kinase
1to6 – GK – Neisseria meningitides
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Eran Hodis
