Homocitrate synthase

spinqualitylabelsall models Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions 3ivt Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Homocitrate synthase (HS) participates in lysine biosynthesis and pyruvate metabolism. HS catalyzes the conversion of acetyl-CoA + H2O + 2-oxoglutarate to 2-hydroxybutane-1,2,4-tricarboxylate + CoA. Structural highlights The HS active site is located in the interior of the N-terminal TIM-barrel domain. Active site. The metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate. Water molecules shown as red spheres.

3D Structures of homocitrate synthase

Updated on 27-September-2021

3ivs – fyHS Lys4 – fission yeast
3ivt, 3ivu - fyHS Lys4 + 2-oxoglutarate
3mi3 - fyHS Lys4 + lysine
2ztj – TtHS + α-ketoglutarate – Thermus thermophilus
2zyf - TtHS + α-ketoglutarate + Mg
2ztk – TtHS + homocitrate
3a9i – TtHS + lysine
6ktq - HS + -ketoglutarate + CoA – Sulfolobus acidocaldarius

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Michal Harel, Alexander Berchansky