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 shirakihara-1997-1 The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shirakihara Y., Leslie AG., Abrahams JP., Walker JE., Ueda T., Sekimoto Y., Kambara M., Saika K., Kagawa Y., Yoshida M. Structure (0969-2126) 1997 atpa_bacp3 ATP synthase subunit alpha atpA F-ATPase subunit alpha ATP synthase F1 sector subunit alpha protein protein bacp3 Bacillus sp. (strain PS3) MSIRAEEISALIKQQIENYESQIQVSDVGTVIQVGDGIARAHGLDNVMSGEAVEFANAVMGMALNLEENNVGIVILGPYTGIKEGDEVRRTGRIMEVPVGETLIGRVVNPLGQPVDGLGPVETTETRPIESRAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTSVAIDTIINQKDQNMICIYVAIGQKESTVATVVETLAKHGAPDYTIVVTASASQPAPLLFLAPYAGVAMGEYFMIMGKHVLVVIDDLSKQAAAYRQLSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIKAMKKVAGTLRLDLAAYRELEAFAQFGSDLDKATQANVARGARTVEVLKQDLHQPIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLWLDQNGQHLLEHIRTTKDLPNEDDLNQAIEAFKKTFVVSQ mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit atpb_bacp3 ATP synthase subunit beta atpD F-ATPase subunit beta ATP synthase F1 sector subunit beta protein protein bacp3 Bacillus sp. (strain PS3) MTRGRVIQVMGPVVDVKFENGHLPAIYNALKIQHKARNENEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVIDTGAPISVPVGQVTLGRVFNVLGEPIDLEGDIPADARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDGLLFIDNIFRFTQAGSEVSALLGRMPSAIGYQPTLATEMGQLQERITSTAKGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLVSTSRALAPEIVGEEHYQVARKVQQTLERYKELQDIIAILGMDELSDEDKLVVHRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILEGKYDHLPEDRFRLVGRIEEVVEKAKAMGVEV mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits atpa-atpd-3 101109 atpa_bacp3 101110 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 atpb_bacp3 101111 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 1sky, P09219 is chain B and P07677 is chain E Resolution 3.200 mint