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EBI PDBe PDBeView

PDBe Entry: 1qlt view

STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE
Summary
Header FLAVOENZYMEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 21.2%, Free R-factor: 26.4%, Spacegroup: I 4
Released 20/09/1999, deposition: 16/09/1999, last revision: 24/02/2009
Authors Mattevi, A.search; Fraaije, M.search
Primary citation Covalent Flavinylation is Essential for Efficient Redox Catalysis in Vanillyl-Alcohol Oxidase.
J.BIOL.CHEM.search vol:274, pag:35514 (2000) [PubMed ID 10585424 ]search
Keywords OXIDOREDUCTASEsearch, FLAVOPROTEINsearch, METHANOL UTILIZATIONsearch, PEROXISOMEsearch, FLAVOENZYMEsearch, OXIDASEsearch, CATALYSISsearch
EC 1.1.3.38 ExPASy BRENDA search (A B)
Organism Penicillium simplicissimum 69488search(A B)
UniProt Vanillyl-alcohol oxidase (EC 1.1.3.38) (Aryl-alcohol oxidase) (4-allylphenol oxidase) P56216search (A B)
Solvent A, B
Related entries 1qlu, 1ahu, 1ahv, 1ahz, 1vao, 2vao
Polymers
Id Name Type UniProt Residues Observed
A, B VANILLYL-ALCOHOL OXIDASE Protein P56216 (VAOX_PENSI)search
 560 98%
Heterogens
Id Name Ligands
A, B FLAVIN-ADENINE DINUCLEOTIDE FAD search
A, B ACETATE ION ACT search
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