4Q3W

Crystal structure of C. violaceum phenylalanine hydroxylase D139E mutation

Summary for 4Q3W

Entry DOI	10.2210/pdb4q3w/pdb
Related	1LTV 3TK4 4Q3W 4Q3X 4Q3Y 4Q3Z
Descriptor	Phenylalanine-4-hydroxylase, COBALT (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywords	mutation, hydroxylase, phenylalanine hydroxylase, kinetics, metals, chromobacterium, phenylketonurias, biopterin, mixed alpha helix-beta sheet, oxidoreductase
Biological source	Chromobacterium violaceum
Total number of polymer chains	1
Total formula weight	33782.04
Authors	Ronau, J.A.,Abu-Omar, M.M.,Das, C. (deposition date: 2014-04-12, release date: 2015-02-18, Last modification date: 2023-09-20)
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 Cited by PubMed: 25295853 DOI: 10.1021/bi500734h PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.4 Å)

Structure validation