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 anonymous-2014q-1 The substrate specificity, enantioselectivity and structure of the (R)-selective amine:pyruvate transaminase from Nectria haematococca in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined J.ward@ucl.ac.uk 2014 imex curation Sayer C., Martinez-Torres R.J., Richter N., Isupov M.N., Hailes H.C., Littlechild J.A., Ward J.M. FEBS J. (1742-464X) Only protein-protein interactions c7yvl8_fusv7 NECHADRAFT_29730 protein protein nech7 Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) Fusarium solani subsp. pisi MATMDKVFAGYAERQAVLEASKNPLAKGVAWIQGELVPLHEARIPLLDQGFMHSDLTYDVPSVWDGRFFRLEDHLNRLEASCKKMRLRMPLPREEVIKTLVDMVAKSGIRDAFVELIVTRGLTGVRGAKPEELLNNNLYMFIQPYVWVMDPDVQYTGGRAIVARTVRRVPPGSIDPTIKNLQWGDLVRGLFEANDRGATYPFLTDGDANLTEGSGFNVVLIKDGVLYTPDRGVLQGITRKSVIDAARSCGYEIRVEHVPIEATYQADEILMCTTAGGIMPITTLDDKPVKDGKVGPITKAIWDRYWAMHWEDEFSFKINY c7yvl8 1511658 n/a TAm 1511659 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false t2 f2a n. The asymmetric unit of the holoenzyme contains the catalytic dimeric molecule of the Nectria Tam (Figure 2a). The gabaculine complex crystals contain only one subunit of TAm, with two subunits of the molecular dimer related by the crystallographic dyad.