5LAT
HIF prolyl hydroxylase 2 (PHD2/EGLN1) P317R variant in complex with Mn(II) and N-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine (IOX3/UN9)
Summary for 5LAT
Entry DOI | 10.2210/pdb5lat/pdb |
Related | 3HQR 4BQX 5L9B 5L9R 5L9V 5LA9 5LAS |
Descriptor | Egl nine homolog 1, MANGANESE (II) ION, N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE, ... (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) |
Cellular location | Cytoplasm : Q9GZT9 |
Total number of polymer chains | 1 |
Total formula weight | 28645.73 |
Authors | Chowdhury, R.,Schofield, C.J. (deposition date: 2016-06-15, 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 Cited by PubMed: 27561929DOI: 10.1038/ncomms12673 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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