5MXJ
Structure of the Y108F mutant of vanillyl alcohol oxidase
Summary for 5MXJ
Entry DOI | 10.2210/pdb5mxj/pdb |
Descriptor | Vanillyl-alcohol oxidase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (4 entities in total) |
Functional Keywords | vanillyl alcohol oxidase, y108f mutant, oxidoreductase |
Biological source | Penicillium simplicissimum |
Cellular location | Peroxisome : P56216 |
Total number of polymer chains | 2 |
Total formula weight | 128029.62 |
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: 2017-01-23, 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: 28717004DOI: 10.1074/jbc.M117.778449 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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