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 Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell (0092-8674) 1998 Ditzel L., Löwe J., Stock D., Stetter KO., Huber H., Huber R., Steinbacher S. no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Ditzel L., Löwe J., Stock D., Stetter KO., Huber H., Huber R., Steinbacher S. no Cell (0092-8674) 1998 thsa_theac Thermosome subunit alpha thsA Ta0980 Thermosome subunit 1 Chaperonin subunit alpha protein protein theac Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) MMTGQVPILVLKEGTQREQGKNAQRNNIEAAKAIADAVRTTLGPKGMDKMLVDSIGDIIISNDGATILKEMDVEHPTAKMIVEVSKAQDTAVGDGTTTAVVLSGELLKQAETLLDQGVHPTVISNGYRLAVNEARKIIDEIAEKSTDDATLRKIALTALSGKNTGLSNDFLADLVVKAVNAVAEVRDGKTIVDTANIKVDKKNGGSVNDTQFISGIVIDKEKVHSKMPDVVKNAKIALIDSALEIKKTEIEAKVQISDPSKIQDFLNQETNTFKQMVEKIKKSGANVVLCQKGIDDVAQHYLAKEGIYAVRRVKKSDMEKLAKATGAKIVTDLDDLTPSVLGEAETVEERKIGDDRMTFVMGCKNPKAVSILIRGGTDHVVSEVERALNDAIRVVAITKEDGKFLWGGGAVEAELAMRLAKYANSVGGREQLAIEAFAKALEIIPRTLAENAGIDPINTLIKLKAEHEKGRISVGVDLDNNGVGDMKAKGVVDPLRVKTHALESAVEVATMILRIDDVIASKKSTPPSGQGGQGQGMPGGGMPEY Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity mint 0E0B3241DF62C63C thsb_theac Thermosome subunit beta thsB Ta1276 Thermosome subunit 2 Chaperonin subunit beta protein protein theac Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) MIAGQPIFILKEGTKRESGKDAMKENIEAAIAISNSVRSSLGPRGMDKMLVDSLGDIVITNDGVTILKEMDVEHPAAKMMVEVSKTQDSFVGDGTTTAVIIAGGLLQQAQGLINQNVHPTVISEGYRMASEEAKRVIDEISTKIGADEKALLLKMAQTSLNSKSASVAKDKLAEISYEAVKSVAELRDGKYYVDFDNIQVVKKQGGAIDDTQLINGIIVDKEKVHPGMPDVVKDAKIALLDAPLEIKKPEFDTNLRIEDPSMIQKFLAQEENMLREMVDKIKSVGANVVITQKGIDDMAQHYLSRAGIYAVRRVKKSDMDKLAKATGASIVSTIDEISSSDLGTAERVEQVKVGEDYMTFVTGCKNPKAVSILVRGETEHVVDEMERSITDSLHVVASALEDGAYAAGGGATAAEIAFRLRSYAQKIGGRQQLAIEKFADAIEEIPRALAENAGLDPIDILLKLRAEHAKGNKTYGINVFTGEIEDMVKNGVIEPIRVGKQAIESATEAAIMILRIDDVIATKSSSSSSNPPKSGSSSESSED mint Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity F9CDAEE63E8B84E6 thsa-thsb 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1a6d, P48424 is chain A and P48425 is chain B Resolution 2.600 mint