5LA9

HIF prolyl hydroxylase 2 (PHD2-R281C/V314C) cross-linked to HIF-1alpha NODD-L397C/D412C and N-oxalylglycine (NOG) (complex-2)

Summary for 5LA9

• Entry DOI: 10.2210/pdb5la9/pdb
• Related: 3HQR 4BQY 5L9B 5L9R 5L9V
• Descriptor: Egl nine homolog 1, Hypoxia-inducible factor 1-alpha, MANGANESE (II) ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, non-heme dioxygenase, iron, 2-oxoglutarate, hypoxia-inducible factor, hif, hif prolyl hydroxylase domain 2, phd2, egln1, oxygenase, hypoxia, dna-binding, metal-binding, transcription, helix-loop-helix-beta, dsbh, facial triad, cytoplasm, transcription/epigenetic regulation, signaling, development, cell structure, beta-hydroxylation, transcription activator/inhibitor, ubl conjugation, polymorphism, vitamin c, zinc-finger, familial erythrocytosis, breast cancer, transcription complex
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : Q9GZT9 Q16665
• Total number of polymer chains: 4
• Total formula weight: 60147.96

Authors

Chowdhury, R.,Schofield, C.J. (deposition date: 2016-06-14, release date: 2016-08-31, Last modification date: 2024-01-10)

• Primary citation: Chowdhury, R.,Leung, I.K.,Tian, Y.M.,Abboud, M.I.,Ge, W.,Domene, C.,Cantrelle, F.X.,Landrieu, I.,Hardy, A.P.,Pugh, C.W.,Ratcliffe, P.J.,Claridge, T.D.,Schofield, C.J.; Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.; Nat Commun, 7:12673-12673, 2016; PubMed: 27561929; DOI: 10.1038/ncomms12673

Experimental method

X-RAY DIFFRACTION (2.813 Å)