1vao Summary

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STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE

The structure was published by Mattevi, A., Fraaije, M.W., Mozzarelli, A., Olivi, L., Coda, A., and van Berkel, W.J., in 1997 in a paper entitled "Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of VANILLYL-ALCOHOL OXIDASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homooctamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A VANILLYL-ALCOHOL OXIDASE P56216 (1-560) (VAOX_PENSI)search Penicillium simplicissimumsearch 100% 560 98%
B VANILLYL-ALCOHOL OXIDASE P56216 (1-560) (VAOX_PENSI)search Penicillium simplicissimumsearch 100% 560 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P56216 (1 - 560) VANILLYL-ALCOHOL OXIDASE Penicillium simplicissimum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P56216) Vanillyl-alcohol oxidase-likesearch, FAD-linked oxidases, N-terminal domainsearch Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2search, Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3search, Vanillyl-alcohol Oxidase; Chain A, domain 3search, Vanillyl-alcohol Oxidase; Chain A, domain 4search PF01565: FAD binding domainsearch, PF02913: FAD linked oxidases, C-terminal domainsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A, B (P56216) cytoplasmsearch peroxisomesearch methanol metabolic processsearch oxidation-reduction processsearch flavin adenine dinucleotide bindingsearch catalytic activitysearch UDP-N-acetylmuramate dehydrogenase activitysearch oxidoreductase activitysearch vanillyl-alcohol oxidase activitysearch oxidoreductase activity, acting on CH-OH group of donorssearch

Chain InterPro annotation
A, B FAD-linked oxidase, C-terminalsearch FAD linked oxidase, N-terminalsearch FAD-linked oxidase-like, C-terminalsearch FAD-binding, type 2search FAD-binding, type 2, subdomain 1search CO dehydrogenase flavoprotein-like, FAD-binding, subdomain 2search Vanillyl-alcohol oxidase/Cytokinin dehydrogenase C-terminal domainsearch Vanillyl-alcohol oxidase, C-terminal subdomain 2search