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 Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering. Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering. FEBS Lett. (0014-5793) 2013 Mehtälä ML., Haataja TJ., Blanchet CE., Hiltunen JK., Svergun DI., Glumoff T. in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Mehtälä ML., Haataja TJ., Blanchet CE., Hiltunen JK., Svergun DI., Glumoff T. FEBS Lett. (0014-5793) 2013 dhb4_drome Peroxisomal multifunctional enzyme type 2 Mfe2 CG3415 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MSSSDGKLRYDGRVAVVTGAGAGLGREYALLFAERGAKVVVNDLGGTHSGDGASQRAADIVVDEIRKAGGEAVADYNSVIDGAKVIETAIKAFGRVDILVNNAGILRDRSLVKTSEQDWNLVNDVHLKGSFKCTQAAFPYMKKQNYGRIIMTSSNSGIYGNFGQVNYTAAKMGLIGLANTVAIEGARNNVLCNVIVPTAASRMTEGILPDILFNELKPKLIAPVVAYLCHESCEDNGSYIESAAGWATKLHMVRGKGAVLRPSLDDPVTIEYVKDVWSNVTDMSKAKHLGAIAEASGTLLEVLEKLKEGGGDAIEDAFEFNSKELITYALGIGASVKNAKDMRFLYENDADFAAIPTFFVLPGLLLQMSTDKLLSKALPNSQVDFSNILHGEQYLEIVDDLPTSGTLLTNGKVFDVMDKGSGAVVVTNSESFDESGRLLVRNQSTTFIVGAGKFGGKKDPIAGVVPLQPAPNRQPDATVQYTTSEDQAALYRLSGDKNPLHIDPQMALLAGFKTPILHGLCTLGFSVRAVLAQFADNNPALFKAVKVRFSGPVIPGQTLRVDLWKQGTRINFRTVVVETGKEVISGAYVDLKSSQAKL 24205DE78964319A q21481_caeel CELE_M03A8.1 dhs-28 M03A8.1 protein protein caeel Caenorhabditis elegans MSLRFDGKVAIVTGAGGGLGKTYALELAKRGCKVVVNDLGGDRHGTSSSSSMADKVVQEIKSAGGQAVANYDSVEFGDKIVKTAIDNFGRIDIVINNAGILRDVSFLKMTELDWDLIFKVHVKGAYAVTKAAWPYMRDQKYGRIVVTSSNAGVHGNFGQANYAAAKSALIGLSNSLAQEGAKYNILANTLVPTAGSRLTETVMPQNLVDALKPDYVTPLVTYMVHDSFEESGKVFEAGAGWYGTIQYYKSKGKVISHASADDIAKNWSTITNMNGAEYIGTITEQSARLVSILEEHEASSGSSSASSGASSGGAFPSNIRSSALFQEMADGVKADPTAVKTLKSIVLYIITDGKNELGKFTLDFKSASPSVYLGDVKNGEKANATVTVADSDFVDIAAGKLNAQKAFMSGKLKVKGNVMLLQKLQTVLEKAKKSKL mint 2DBD94562A09BE55 dhb4_human Peroxisomal multifunctional enzyme type 2 HSD17B4 EDH17B4 D-bifunctional protein 17-beta-hydroxysteroid dehydrogenase 4 Multifunctional protein 2 SDR8C1 Short chain dehydrogenase/reductase family 8C member 1 protein protein human Homo sapiens Human MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLSKIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKDLKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKVAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL 7B11E02483328BCE mfe2 1 DmMFE-2 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f2 mint The crystal structure of DmMFE-2 is known at 2.15 Å resolution [15]. It forms a compact double dimeric‟ structure in which both the dehydrogenase and the hydratase 2 from different MFE-2 monomers form dimers (Fig. 2). SAXS structure of DmMFE-2 and its fit with the crystal structure would indicate the value of using DmMFE-2 as a framework for the human protein, which in addition contains the SCP-2L domain in each MFE-2 monomer. SAXS data were collected from the full-length DmMFE-2, the dehydrogenase domain (DmDH), the hydratase 2 domain (DmH2) and the two catalytic domains together in the same solution. In the SAXS models the locations of the enzyme dimers could easily be determined, yet the low resolution does not allow to unambiguously differentiating between the dehydrogenase dimer and the hydratase 2 dimer. hsd17b4-1 1 HsMFE-2 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f3 mint In the SAXS models the locations of the enzyme dimers could easily be determined, yet the low resolution does not allow to unambiguously differentiating between the dehydrogenase dimer and the hydratase 2 dimer. dhs-1 1 CeMFE-2 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f4 mint In the SAXS models the locations of the enzyme dimers could easily be determined, yet the low resolution does not allow to unambiguously differentiating between the dehydrogenase dimer and the hydratase 2 dimer.