3ouh

PHD2-R127 with JNJ41536014PHD2-R127 with JNJ41536014

Structural highlights 3ouh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.51Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed HIF prolyl 4-hydroxylases (PHD) are a family of enzymes that mediate key physiological responses to hypoxia by modulating the levels of hypoxia inducible factor 1-alpha (HIF1alpha). Certain benzimidazole-2-pyrazole carboxylates were discovered to be PHD2 inhibitors using ligand- and structure-based methods and found to be potent, orally efficacious stimulators of erythropoietin secretion in vivo. Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues.,Rosen MD, Venkatesan H, Peltier HM, Bembenek SD, Kanelakis KC, Zhao LX, Leonard BE, Hocutt FM, Wu X, Palomino HL, Brondstetter TI, Haugh PV, Cagnon L, Yan W, Liotta LA, Young A, Mirzadegan T, Shankley NP, Barrett TD, Rabinowitz MH ACS Med Chem Lett. 2010 Oct 5;1(9):526-9. doi: 10.1021/ml100198y. eCollection, 2010 Dec 9. PMID:24900242 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Polyl hydroxylase domain 3D structures Prolyl hydroxylase domain

spinqualitylabelsall models 3ouh, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image