4GAP

Structure of the Ndi1 protein from Saccharomyces cerevisiae in complex with NAD+

Summary for 4GAP

• Entry DOI: 10.2210/pdb4gap/pdb
• Related: 4G9K 4GAV
• Descriptor: Rotenone-insensitive NADH-ubiquinone oxidoreductase, FLAVIN-ADENINE DINUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: nucleotide-binding domains, membrane, oxidoreductase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P32340
• Total number of polymer chains: 2
• Total formula weight: 108499.07

Authors

Iwata, M.,Lee, Y.,Yamashita, T.,Yagi, T.,Iwata, S.,Cameron, A.D.,Maher, M.J. (deposition date: 2012-07-25, release date: 2012-09-05, Last modification date: 2024-02-28)

• Primary citation: Iwata, M.,Lee, Y.,Yamashita, T.,Yagi, T.,Iwata, S.,Cameron, A.D.,Maher, M.J.; The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates.; Proc.Natl.Acad.Sci.USA, 109:15247-15252, 2012; PubMed: 22949654; DOI: 10.1073/pnas.1210059109

Experimental method

X-RAY DIFFRACTION (2.9 Å)