#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:Q5SIY4	uniprotkb:Q5SIY4	intact:EBI-9699580|ensemblbacteria:BAD71053	intact:EBI-9699580|ensemblbacteria:BAD71053	psi-mi:leu3_thet8(display_long)|uniprotkb:leuB(gene name)|psi-mi:leuB(display_short)|uniprotkb:3-IPM-DH(gene name synonym)|uniprotkb:Beta-IPM dehydrogenase(gene name synonym)|uniprotkb:TTHA1230(locus name)	psi-mi:leu3_thet8(display_long)|uniprotkb:leuB(gene name)|psi-mi:leuB(display_short)|uniprotkb:3-IPM-DH(gene name synonym)|uniprotkb:Beta-IPM dehydrogenase(gene name synonym)|uniprotkb:TTHA1230(locus name)	psi-mi:"MI:0114"(x-ray crystallography)	Palló et al. (2014)	imex:IM-23181|pubmed:25211160	taxid:300852(thet8)|taxid:300852("Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)")	taxid:300852(thet8)|taxid:300852("Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)")	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-9699577|imex:IM-23181-1	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	rcsb pdb:4WUO|refseq:WP_011228534.1|interpro:IPR019818|interpro:IPR024084|interpro:IPR004429(3-isopropylmalate dehydrogenase)|refseq:YP_144496.1|rcsb pdb:1DPZ|rcsb pdb:1DR0|rcsb pdb:1DR8|rcsb pdb:1G2U|rcsb pdb:1GC8|rcsb pdb:1GC9|rcsb pdb:1HEX|rcsb pdb:1IDM|rcsb pdb:1IPD|rcsb pdb:1OSI|rcsb pdb:1OSJ|rcsb pdb:1XAA|rcsb pdb:1XAB|rcsb pdb:1XAC|rcsb pdb:1XAD|rcsb pdb:2Y3Z|rcsb pdb:2Y40|rcsb pdb:2Y41|rcsb pdb:2Y42|rcsb pdb:2ZTW|rcsb pdb:4F7I|ensemblbacteria:BAD71053(gene)|ensemblbacteria:BAD71053(transcript)|go:"GO:0000287"(magnesium ion binding)|go:"GO:0003862"(3-isopropylmalate dehydrogenase activity)|go:"GO:0005737"(cytoplasm)|go:"GO:0009082"(branched-chain amino acid biosynthetic process)|go:"GO:0009098"(leucine biosynthetic process)|go:"GO:0042802"(identical protein binding)|go:"GO:0051287"(NAD binding)	rcsb pdb:4WUO|refseq:WP_011228534.1|interpro:IPR019818|interpro:IPR024084|interpro:IPR004429(3-isopropylmalate dehydrogenase)|refseq:YP_144496.1|rcsb pdb:1DPZ|rcsb pdb:1DR0|rcsb pdb:1DR8|rcsb pdb:1G2U|rcsb pdb:1GC8|rcsb pdb:1GC9|rcsb pdb:1HEX|rcsb pdb:1IDM|rcsb pdb:1IPD|rcsb pdb:1OSI|rcsb pdb:1OSJ|rcsb pdb:1XAA|rcsb pdb:1XAB|rcsb pdb:1XAC|rcsb pdb:1XAD|rcsb pdb:2Y3Z|rcsb pdb:2Y40|rcsb pdb:2Y41|rcsb pdb:2Y42|rcsb pdb:2ZTW|rcsb pdb:4F7I|ensemblbacteria:BAD71053(gene)|ensemblbacteria:BAD71053(transcript)|go:"GO:0000287"(magnesium ion binding)|go:"GO:0003862"(3-isopropylmalate dehydrogenase activity)|go:"GO:0005737"(cytoplasm)|go:"GO:0009082"(branched-chain amino acid biosynthetic process)|go:"GO:0009098"(leucine biosynthetic process)|go:"GO:0042802"(identical protein binding)|go:"GO:0051287"(NAD binding)	rcsb pdb:4F7I	-	-	figure legend:t1 t2 f1|comment:"The four individual protein chains in the   asymmetric unit of the crystal are very similar to each other with r.m.s. differences between the chains   of about 0.2 Å, which is not significantly larger than the overall coordinate error of the structure. Each   of the four chains harbors one NADH, one IPM, one Mn2+ and two K+   ions, one of them bound close   to the active site. The chains A-D assemble into two functional dimers (AB and CD), which both   exhibit a fully closed conformation, only slightly better closed than the previously published structure   of the ternary complex Tt-IPMDH-Mn2+-IPM [17]. Overlaying of the various open, partially and fully   closed forms are illustrated by Fig. 2A and 2B. The very same closed conformation was observed in a   different crystal form (data not shown), which lends support to the biological relevance of this   conformation."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2014/09/08	2014/10/16	rogid:wNLgN6gU4MoaQ8IhJmvD0SLCOxo300852	rogid:wNLgN6gU4MoaQ8IhJmvD0SLCOxo300852	intact-crc:6A220F537A4DEF4C|rigid:zcISa5zJh0PXQCaMcZN2J43Fds4	false	his tag:?-?	his tag:?-?	2	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)