6N1K
Full-length human phenylalanine hydroxylase (PAH) in the resting state
Summary for 6N1K
Entry DOI | 10.2210/pdb6n1k/pdb |
Descriptor | Phenylalanine-4-hydroxylase, CHLORIDE ION, FE (III) ION, ... (4 entities in total) |
Functional Keywords | resting-state pah, allosterically controlled aromatic amino acid hydroxylase, oxidoreductase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 4 |
Total formula weight | 207491.78 |
Authors | Arturo, E.C.,Jaffe, E.K. (deposition date: 2018-11-08, release date: 2019-05-22, Last modification date: 2023-10-11) |
Primary citation | Arturo, E.C.,Gupta, K.,Hansen, M.R.,Borne, E.,Jaffe, E.K. Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium. J.Biol.Chem., 294:10131-10145, 2019 Cited by PubMed: 31076506DOI: 10.1074/jbc.RA119.008294 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.057 Å) |
Structure validation
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