5MXU

Structure of the Y503F mutant of vanillyl alcohol oxidase

Summary for 5MXU

Entry DOI	10.2210/pdb5mxu/pdb
Descriptor	Vanillyl-alcohol oxidase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (4 entities in total)
Functional Keywords	vanillyl alcohol oxidase, y503f mutant, oxidoreductase
Biological source	Penicillium simplicissimum
Cellular location	Peroxisome : P56216
Total number of polymer chains	2
Total formula weight	127937.53
Authors	Ewing, T.A.,Nguyen, Q.-T.,Allan, R.C.,Gygli, G.,Romero, E.,Binda, C.,Fraaije, M.W.,Mattevi, A.,van Berkel, W.J.H. (deposition date: 2017-01-24, release date: 2017-07-26, Last modification date: 2024-01-17)
Primary citation	Ewing, T.A.,Nguyen, Q.T.,Allan, R.C.,Gygli, G.,Romero, E.,Binda, C.,Fraaije, M.W.,Mattevi, A.,van Berkel, W.J.H. Two tyrosine residues, Tyr-108 and Tyr-503, are responsible for the deprotonation of phenolic substrates in vanillyl-alcohol oxidase. J. Biol. Chem., 292:14668-14679, 2017 Cited by PubMed: 28717004 DOI: 10.1074/jbc.M117.778449 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation