1d4a Summary

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CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION

The structure was published by Faig, M., Bianchet, M.A., Talalay, P., et al., Winski, S., Ross, D., and Amzel, L.M., in 2000 in a paper entitled "Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of QUINONE REDUCTASE.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 QUINONE REDUCTASE P15559 (2-274) (NQO1_HUMAN)search Homo sapienssearch 99% 273 100%
B QUINONE REDUCTASE P15559 (2-274) (NQO1_HUMAN)search Homo sapienssearch 99% 273 100%
C QUINONE REDUCTASE P15559 (2-274) (NQO1_HUMAN)search Homo sapienssearch 99% 273 100%
D QUINONE REDUCTASE P15559 (2-274) (NQO1_HUMAN)search Homo sapienssearch 99% 273 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P15559 (2 - 274) QUINONE REDUCTASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P15559) Quinone reductasesearch Rossmann foldsearch PF02525: Flavodoxin-like foldsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B, C, D (P15559) extracellular vesicular exosomesearch cytosolsearch cytoplasmsearch neuronal cell bodysearch poly(A) RNA bindingsearch superoxide dismutase activitysearch oxidoreductase activitysearch NAD(P)H dehydrogenase (quinone) activitysearch cytochrome-b5 reductase activity, acting on NAD(P)Hsearch protein bindingsearch response to ethanolsearch response to nutrientsearch response to oxidative stresssearch synaptic transmission, cholinergicsearch removal of superoxide radicalssearch response to organic cyclic compoundsearch superoxide metabolic processsearch nitric oxide biosynthetic processsearch positive regulation of neuron apoptotic processsearch xenobiotic metabolic processsearch response to estradiolsearch negative regulation of catalytic activitysearch oxidation-reduction processsearch regulation of cellular amino acid metabolic processsearch agingsearch small molecule metabolic processsearch response to toxic substancesearch cellular nitrogen compound metabolic processsearch

Chain InterPro annotation
A, B, C, D Flavodoxin-like foldsearch Flavoprotein-likesearch