Prolyl hydroxylase domain-containing protein

spinqualitylabelsall models Human PHD2 catalytic domain complex with Fe+2 ion (orange), inhibitor and sulfate, 3ouh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D See also Hydroxylase Prolyl hydroxylase domain-containing protein (PHD) or egl nine homolog 1 or PHD2 or EGLN1 proteins mediate oxygen-dependent degradation of Hypoxia-inducible factor (HIF) α subunit. They include PHD1, PHD2 and PHD3. The PHD is a Fe+2/oxogluterate (2OG)-dependent enzyme. 3ouh is the crystallized structure of the enzyme PHD2, an oxidoreductase that is 237 amino acids long with a molecular weight of 27 kDa. 3ouh is found in Homo sapiens and is a homolog of EGLN1 found in C. elegans. The protein has three ligands: O14 (a 1-(5-chloro-6-fluoro-1H-benzimidazol-2-yl)-1H-pyrazole-4-carboxylic acid), Fe+2 (an iron ion), and SO4 (a sulfate ion). Water molecules are shown as red spheres. It is involved in mediating physiological responses to hypoxia by degrading the transcription factor of a hypoxia-inducible factor HIF1-α. In hypoxic conditions, the activity of PHD2 lessens, causing an increase in HIF1-α, resulting in secretion of erythropoietin, anaerobic glycolysis, and angiogenesis. For more detalis see Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme. 3D Structures of prolyl hydroxylase domain Polyl hydroxylase domain 3D structures

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