Glycerate kinase

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[[Image:1to6.png|left|200px|thumb|Crystal Structure of glycerate kinase, [[1to6]]]]
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{{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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'''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.
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'''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.
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== 3D Structures of glycerate kinase ==
== 3D Structures of glycerate kinase ==

Revision as of 10:06, 18 August 2014

Template:STRUCTURE 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.

3D Structures of glycerate kinase

Updated on 18-August-2014

1to6 – GK – Neisseria meningitides

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Eran Hodis

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