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Prolyl hydroxylase domain

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**[[6st3]] - hPHD2 catalytic domain + Mn + pyrimidin derivative<br />
**[[6st3]] - hPHD2 catalytic domain + Mn + pyrimidin derivative<br />
**[[6yvt]] - hPHD2 catalytic domain + Mn + pyridin derivative<br />
**[[6yvt]] - hPHD2 catalytic domain + Mn + pyridin derivative<br />
-
**[[6qgv]], [[5a3u]] - hPHD2 catalytic domain + Mn + inhibitor<br />
+
**[[6qgv]], [[5a3u]], [[6st3]], [[6yvt]], [[6zbn]], [[6zbo]] - hPHD2 catalytic domain + Mn + inhibitor<br />
**[[5ox6]], [[6ox5]] - hPHD2 catalytic domain + Mn + drug<br />
**[[5ox6]], [[6ox5]] - hPHD2 catalytic domain + Mn + drug<br />
**[[5lat]], [[5lb6]], [[5lbb]], [[5lbc]], [[5lbe]], [[5lbf]], [[4uwd]] - hPHD2 catalytic domain (mutant) + Mn + quinolin derivative<br />
**[[5lat]], [[5lb6]], [[5lbb]], [[5lbc]], [[5lbe]], [[5lbf]], [[4uwd]] - hPHD2 catalytic domain (mutant) + Mn + quinolin derivative<br />
-
**[[4h6j]] – hPHD Pasb domain 238-348 (mutant) + aryl hydrocarbon nuclear translocator (mutant)<br />
+
**[[6yvx]], [[6yvz]] - hPHD2 catalytic domain + Mn + peptide<br />
 +
**[[6yw3]] - hPHD2 catalytic domain + Mn + peptide + oxalylglycine<br />
 +
**[[6yw1]], [[6yw2]], [[6yw4]] - hPHD2 catalytic domain (mutant) + Mn + peptide + oxalylglycine<br />
*Prolyl hydroxylase domain containing other metal ions
*Prolyl hydroxylase domain containing other metal ions
-
**[[2y33]] – hPHD2 catalytic domain residues 181-426 + Zn + quinolin derivative – human<br />
+
**[[2y33]] – hPHD2 catalytic domain residues + Zn + quinolin derivative – human<br />
-
**[[3ouh]], [[3oui]], [[5v18]] - hPHD2 catalytic domain + Fe + inhibitor<br />
+
**[[3ouh]], [[3oui]], [[5v18]], [[6nmq]], [[6yvw]], [[6yw0]] - hPHD2 catalytic domain + Fe + inhibitor<br />
**[[4kbz]] - hPHD2 catalytic domain (mutant) + Fe + inhibitor<br />
**[[4kbz]] - hPHD2 catalytic domain (mutant) + Fe + inhibitor<br />
**[[4jzr]] - hPHD2 catalytic domain + Ni + inhibitor<br />
**[[4jzr]] - hPHD2 catalytic domain + Ni + inhibitor<br />

Revision as of 11:00, 1 February 2022

Human PHD2 catalytic domain complex with Fe+2 ion (orange), inhibitor and sulfate, 3ouh

Drag the structure with the mouse to rotate

3D Structures of prolyl hydroxylase domain

Updated on 01-February-2022

References

  1. Stolze IP, Mole DR, Ratcliffe PJ. Regulation of HIF: prolyl hydroxylases. Novartis Found Symp. 2006;272:15-25; discussion 25-36. PMID:16686427
  2. Rosen M D, Venkatesan H, Peltier H M, Bembenek S D, Kanelakis K C, Zhao L X, Leonard B E, Hocutt F M, Wu X, Palomino H L, Brondtetter T I, Haugh P V, Cagnon L, Yan W, Liotta L A, Young A, Mirzadegan T, Shankley N P, Barrett T D, Rabinowitz M H. Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues. ACS Medicinal Chemical Letters. 2010 Oct 5.


Created with the participation of Andrew Winslow.

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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