3OUH

PHD2-R127 with JNJ41536014

Summary for 3OUH

• Entry DOI: 10.2210/pdb3ouh/pdb
• Related: 3OUI 3OUJ
• Descriptor: Egl nine homolog 1, FE (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: phd2, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : Q9GZT9
• Total number of polymer chains: 1
• Total formula weight: 27011.83

Authors

Kim, H.,Clark, R. (deposition date: 2010-09-14, release date: 2010-12-01, Last modification date: 2018-04-18)

Primary citation

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.,Brondstetter, 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 Med Chem Lett, 1:526-529, 2010

PubMed Abstract: 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-α (HIF1α). 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.

PubMed: 24900242
DOI: 10.1021/ml100198y

Experimental method

X-RAY DIFFRACTION (2.51 Å)