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

Summary for 6N1K

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 molecular weight207491.78
Arturo, E.C.,Jaffe, E.K. (deposition date: 2018-11-08, release date: 2019-05-22)
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., 2019
PubMed: 31076506 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.RA119.008294
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.2412 0.1% 1.5% 2.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution