5A4K
Crystal structure of the R139W variant of human NAD(P)H:quinone oxidoreductase
Summary for 5A4K
Entry DOI | 10.2210/pdb5a4k/pdb |
Descriptor | NAD(P)H DEHYDROGENASE [QUINONE] 1, FLAVIN-ADENINE DINUCLEOTIDE, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
Functional Keywords | nqo1, fad, flavoprotein, oxidative stress, quinone reductase, drug metabolism, oxidoreductase, single amino acid exchange |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Cytoplasm: P15559 |
Total number of polymer chains | 4 |
Total formula weight | 135992.62 |
Authors | Lienhart, W.D.,Strandback, E.,Gudipati, V.,Uhl, M.K.,Rantase, D.M.,Zangger, K.,Gruber, K.,Macheroux, P. (deposition date: 2015-06-10, release date: 2016-06-29, Last modification date: 2024-01-10) |
Primary citation | Lienhart, W.D.,Strandback, E.,Gudipati, V.,Koch, K.,Binter, A.,Uhl, M.K.,Rantasa, D.M.,Bourgeois, B.,Madl, T.,Zangger, K.,Gruber, K.,Macheroux, P. Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1). FEBS J., 284:1233-1245, 2017 Cited by PubMed: 28236663DOI: 10.1111/febs.14051 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.093 Å) |
Structure validation
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