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6N1K

Full-length human phenylalanine hydroxylase (PAH) in the resting state

Summary for 6N1K
Entry DOI10.2210/pdb6n1k/pdb
DescriptorPhenylalanine-4-hydroxylase, CHLORIDE ION, FE (III) ION, ... (4 entities in total)
Functional Keywordsresting-state pah, allosterically controlled aromatic amino acid hydroxylase, oxidoreductase
Biological sourceHomo sapiens (Human)
Total number of polymer chains4
Total formula weight207491.78
Authors
Arturo, E.C.,Jaffe, E.K. (deposition date: 2018-11-08, release date: 2019-05-22, Last modification date: 2023-10-11)
Primary citationArturo, 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: 31076506
DOI: 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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