MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint leys-2003-1 Extensive conformational sampling in a ternary electron transfer complex. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Leys D., Basran J., Talfournier F., Sutcliffe MJ., Scrutton NS. dl37@le.ac.uk Nat. Struct. Biol. (1072-8368) 2003 etfb_metme Electron transfer flavoprotein subunit beta etfB Electron transfer flavoprotein small subunit protein protein metme Methylophilus methylotrophus MKILVAVKQTAALEEDFEIREDGMDVDEDFMMYDLNEWDDFSLEEAMKIKESSDTDVEVVVVSVGPDRVDESLRKCLAKGADRAVRVWDDAAEGSDAIVVGRILTEVIKKEAPDMVFAGVQSSDQAYASTGISVASYLNWPHAAVVADLQYKPGDNKAVIRRELEGGMLQEVEINCPAVLTIQLGINKPRYASLRGIKQAATKPIEEVSLADIGLSANDVGAAQSMSRVRRMYIPEKGRATMIEGTISEQAAKIIQIINEFKGA mint The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) etfa_metme Electron transfer flavoprotein subunit alpha etfA Electron transfer flavoprotein large subunit protein protein metme Methylophilus methylotrophus MSKILVIAEHRRNDLRPVSLELIGAANGLKKSGEDKVVVAVIGSQADAFVPALSVNGVDELVVVKGSSIDFDPDVFEASVSALIAAHNPSVVLLPHSVDSLGYASSLASKTGYGFATDVYIVEYQGDELVATRGGYNQKVNVEVDFPGKSTVVLTIRPSVFKPLEGAGSPVVSNVDAPSVQSRSQNKDYVEVGGGNDIDITTVDFIMSIGRGIGEETNVEQFRELADEAGATLCCSRPIADAGWLPKSRQVGQSGKVVGSCKLYVAMGISGSIQHMAGMKHVPTIIAVNTDPGASIFTIAKYGIVADIFDIEEELKAQLAA The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) mint etfa-etfb-2 101061 etfb_metme ETFB 101062 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 etfa_metme ETFA 101063 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 direct interaction direct interaction false false false In the xray complex 1o97, P53570 is chain C and P53571 is chain D Resolution 1.600 mint