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Structure paper

TitleBiophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 10131-10145, Year 2019
Publish dateNov 8, 2018 (structure data deposition date)
AuthorsArturo, E.C. / Gupta, K. / Hansen, M.R. / Borne, E. / Jaffe, E.K.
External linksJ. Biol. Chem. / PubMed:31076506
MethodsX-ray diffraction
Resolution3.057 Å
Structure data

PDB-6n1k:
Full-length human phenylalanine hydroxylase (PAH) in the resting state
Method: X-RAY DIFFRACTION / Resolution: 3.057 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-FE:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / resting-state PAH / allosterically controlled aromatic amino acid hydroxylase

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