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: 28236663 DOI: 10.1111/febs.14051 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.093 Å)

Structure validation