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: 27561929 DOI: 10.1038/ncomms12673 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation