Crystal structure of C. violaceum phenylalanine hydroxylase D139E mutation

Summary for 4Q3W

Related3TK4 1LTV 4Q3W 4Q3X 4Q3Y 4Q3Z
DescriptorPhenylalanine-4-hydroxylase, COBALT (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsmutation, hydroxylase, phenylalanine hydroxylase, kinetics, metals, chromobacterium, phenylketonurias, biopterin, mixed alpha helix-beta sheet, oxidoreductase
Biological sourceChromobacterium violaceum
Total number of polymer chains1
Total molecular weight33782.04
Ronau, J.A.,Abu-Omar, M.M.,Das, C. (deposition date: 2014-04-12, release date: 2015-02-18, Last modification date: 2019-11-20)
Primary citation
Ronau, J.A.,Paul, L.N.,Fuchs, J.E.,Liedl, K.R.,Abu-Omar, M.M.,Das, C.
A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis.
Biochemistry, 53:6834-6848, 2014
PubMed: 25295853 (PDB entries with the same primary citation)
DOI: 10.1021/bi500734h
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.19710 0.9% 6.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-08-12