6F4M
Human JMJD5 in its apo form.
Summary for 6F4M
Entry DOI | 10.2210/pdb6f4m/pdb |
Related | 6F4N 6F4O 6F4P 6F4Q 6F4R 6F4S 6F4T |
Descriptor | JmjC domain-containing protein 5 (2 entities in total) |
Functional Keywords | oxidoreductase, non-heme, iron, 2-oxoglutarate, dioxygenase, jmjc, jmjc domain, lysine-specific demethylase 8, jmjc domain-containing protein 5, arginyl c-3 hydroxylase, jmjd5, kdm8, oxygenase, hypoxia, dna-binding, metal-binding, translation, dsbh, facial triad, cytoplasm, jmjc hydroxylase, jmjc demethylase, kdms, post-translational modifications, ptm, beta-hydroxylation, hydroxylation, arginine hydroxylation, rcc1 domain-containing protein 1, rccd1, regulator of chromosome condensation, 40s ribosomal protein s6, rps6, ribosome biogenesis, transcription, epigenetic regulation, signaling, development, cell structure, transcription activator/inhibitor, phosphorylation, cancer, polymorphism |
Biological source | Homo sapiens (Human) |
Cellular location | Nucleus : Q8N371 |
Total number of polymer chains | 1 |
Total formula weight | 27133.61 |
Authors | Chowdhury, R.,Islam, M.S.,Schofield, C.J. (deposition date: 2017-11-29, release date: 2018-04-04, Last modification date: 2024-01-17) |
Primary citation | Wilkins, S.E.,Islam, S.,Gannon, J.M.,Markolovic, S.,Hopkinson, R.J.,Ge, W.,Schofield, C.J.,Chowdhury, R. JMJD5 is a human arginyl C-3 hydroxylase. Nat Commun, 9:1180-1180, 2018 Cited by PubMed: 29563586DOI: 10.1038/s41467-018-03410-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.705 Å) |
Structure validation
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