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1NOX

NADH OXIDASE FROM THERMUS THERMOPHILUS

Summary for 1NOX
Entry DOI10.2210/pdb1nox/pdb
DescriptorNADH OXIDASE, FLAVIN MONONUCLEOTIDE (3 entities in total)
Functional Keywordsflavoenzyme, flavoprotein fmn, oxidoreductase, thermophile
Biological sourceThermus thermophilus
Total number of polymer chains1
Total formula weight23236.80
Authors
Hecht, H.J.,Erdmann, H.,Park, H.J.,Sprinzl, M.,Schmid, R.D. (deposition date: 1996-11-20, release date: 1997-03-12, Last modification date: 2024-04-03)
Primary citationHecht, H.J.,Erdmann, H.,Park, H.J.,Sprinzl, M.,Schmid, R.D.
Crystal structure of NADH oxidase from Thermus thermophilus.
Nat.Struct.Biol., 2:1109-1114, 1995
Cited by
PubMed Abstract: The crystal structures of the flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) containing isoforms of NADH oxidase from Thermus thermophilus have been determined by isomorphous and molecular replacement and refined to 2.3 A and 1.6 A resolution with R-values of 18.5% and 18.6% respectively. The structure of the homodimeric enzyme consists of a central 4-stranded antiparallel beta-sheet covered by helices, a more flexible domain formed by two helices, and a C-terminal excursion connecting the subunits. The active sites are located in a deep cleft between the subunits. The binding site of the flavin cofactor lacks the common nucleotide binding fold and is different from the FMN binding site found in flavodoxins.
PubMed: 8846223
DOI: 10.1038/nsb1295-1109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.59 Å)
Structure validation

237735

数据于2025-06-18公开中

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