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 groth-2001-1 The structure of the chloroplast F1-ATPase at 3.2 A resolution. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Groth G., Pohl E. georg.groth@uniduesseldorf.de J. Biol. Chem. (0021-9258) 2001 atpa_spiol ATP synthase subunit alpha, chloroplastic atpA F-ATPase subunit alpha ATP synthase F1 sector subunit alpha protein protein spiol Spinacia oleracea (Spinach) Spinach MATIRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEAEALLKEAIQEQMERFLLQEQA mint Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit atpb_spiol ATP synthase subunit beta, chloroplastic atpB F-ATPase subunit beta ATP synthase F1 sector subunit beta protein protein spiol Spinacia oleracea (Spinach) Spinach MRINPTTSDPGVSTLEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKLKK 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-atpb-1 100429 atpa_spiol 100430 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_spiol 100431 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 1fx0, P06450 is chain A and P00825 is chain B Resolution 3.200 mint