DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ iwata-2012-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Iwata M., Lee Y., Yamashita T., Yagi T., Iwata S., Cameron AD., Maher MJ. DIP original experiment: DIP-251788X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates. Iwata M., Lee Y., Yamashita T., Yagi T., Iwata S., Cameron AD., Maher MJ. Only protein-protein interactions imex curation ndi1_yeast Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial NDI1 YML120C YM7056.06C NADH:ubiquinone reductase (non-electrogenic) Internal NADH dehydrogenase protein protein yeast Saccharomyces cerevisiae Baker's yeast MLSKNLYSNKRLLTSTNTLVRFASTRSTGVENSGAGPTSFKTMKVIDPQHSDKPNVLILGSGWGAISFLKHIDTKKYNVSIISPRSYFLFTPLLPSAPVGTVDEKSIIEPIVNFALKKKGNVTYYEAEATSINPDRNTVTIKSLSAVSQLYQPENHLGLHQAEPAEIKYDYLISAVGAEPNTFGIPGVTDYGHFLKEIPNSLEIRRTFAANLEKANLLPKGDPERRRLLSIVVVGGGPTGVEAAGELQDYVHQDLRKFLPALAEEVQIHLVEALPIVLNMFEKKLSSYAQSHLENTSIKVHLRTAVAKVEEKQLLAKTKHEDGKITEETIPYGTLIWATGNKARPVITDLFKKIPEQNSSKRGLAVNDFLQVKGSNNIFAIGDNAFAGLPPTAQVAHQEAEYLAKNFDKMAQIPNFQKNLSSRKDKIDLLFEENNFKPFKYNDLGALAYLGSERAIATIRSGKRTFYTGGGLMTFYLWRILYLSMILSARSRLKVFFDWIKLAFFKRDFFKGL E3A43D75A1ADCF3B ndi1-1 3244789 N/A 3244790 unspecified role unspecified role unspecified role unspecified role Region 43-513 Region 43-513 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false