#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)	Gráczer et al. (2015)	pubmed:25497013|imex:IM-23837	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-10634226|imex:IM-23837-1	-	-	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:4wuo	-	-	figure legend:t1 f1|comment:"The global structure of E270A mutant IPMDH with bound Mn2+, IPM and NADH exhibits a closed conformation, but slightly less closed than that of the previously determined [7] wild-type enzyme. However, the active sites exhibit well defined differences due to the mutation. Fig. 1 illustrates part of the active site of Tt-IPMDH with bound IPM and NADH both of the wild-type (A) and the E270A mutant (B) enzymes. In the wild-type enzyme the carboxylate group of E270 is an important electrostatic ligand for K+-ion. In the active site of the wild-type IPMDH there was a peak observed on the Fo Fc difference density map when the K+-ion was initially modelled as water, however in case of the E270A mutant enzyme there was no residual density when this peak was modelled as water."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2015/02/16	2015/02/23	rogid:wNLgN6gU4MoaQ8IhJmvD0SLCOxo300852	rogid:wNLgN6gU4MoaQ8IhJmvD0SLCOxo300852	intact-crc:7151B238600FFD64|rigid:zcISa5zJh0PXQCaMcZN2J43Fds4	false	mutation:270-270	mutation:270-270	2	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)