Prolyl hydroxylase domain

See also Hydroxylase Prolyl hydroxylase domain (PHD) or egl nine homolog 1 (PHD2/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: (a 1-(5-chloro-6-fluoro-1H-benzimidazol-2-yl)-1H-pyrazole-4-carboxylic acid), , 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 Updated on 29-May-2025 {{#tree:id=OrganizedByTopic|openlevels=0| Prolyl hydroxylase domain containing Mn 5l9r - hPHD2 catalytic domain residues 181-426 (mutant) + Mn + 2OG - human 3hqr, 5l9b - hPHD2 catalytic domain (mutant) + Mn + HIF 1 α C terminal + 2OG 5l9v, 5la9, 5las - hPHD2 catalytic domain (mutant) + Mn + HIF NODD domain + 2OG 4bqw, 4bqx, 4bqy - hPHD2 catalytic domain + Mn + quinolin derivative 6st3 - hPHD2 catalytic domain + Mn + pyrimidin derivative 6yvt - hPHD2 catalytic domain + Mn + pyridin derivative 6qgv, 5a3u, 6st3, 6yvt, 6zbn, 6zbo - hPHD2 catalytic domain + Mn + inhibitor 5ox6, 6ox5 - hPHD2 catalytic domain + Mn + drug 5lat, 5lb6, 5lbb, 5lbc, 5lbe, 5lbf, 4uwd - hPHD2 catalytic domain (mutant) + Mn + quinolin derivative 6yvx, 6yvz - hPHD2 catalytic domain + Mn + peptide 6yw3 - hPHD2 catalytic domain + Mn + peptide + oxalylglycine 6yw1, 6yw2, 6yw4 - hPHD2 catalytic domain (mutant) + Mn + peptide + oxalylglycine Prolyl hydroxylase domain containing other metal ions 2y33 – hPHD2 catalytic domain residues + Zn + quinolin derivative – human 3ouh, 3oui, 5v18, 6nmq, 6yvw, 6yw0 - hPHD2 catalytic domain + Fe + inhibitor 4kbz - hPHD2 catalytic domain (mutant) + Fe + inhibitor 4jzr - hPHD2 catalytic domain + Ni + inhibitor 3ouj - hPHD2 catalytic domain + Fe + 2OG 3hqu - hPHD2 catalytic domain + Fe + HIF 1 α C terminal + quinolin derivative 2hbt, 2hbu, 2g19, 2g1m, 2y34, 4bqi - hPHD2 catalytic domain + Fe + quinolin derivative 5v18 - hPHD2 catalytic domain + Fe + pyridin derivative 5v1b - hPHD1 catalytic domain + Fe + inhibitor 6nmq - hPHD2 catalytic domain + Fe + inhibitor }}

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

Created with the participation of Andrew Winslow.