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2ztw
From Proteopedia
(Difference between revisions)
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==Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+== | ==Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+== | ||
<StructureSection load='2ztw' size='340' side='right' caption='[[2ztw]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='2ztw' size='340' side='right' caption='[[2ztw]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuB, TTHA1230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuB, TTHA1230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ztw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ztw OCA], [http://pdbe.org/2ztw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ztw RCSB], [http://www.ebi.ac.uk/pdbsum/2ztw PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ztw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ztw OCA], [http://pdbe.org/2ztw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ztw RCSB], [http://www.ebi.ac.uk/pdbsum/2ztw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ztw ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zt/2ztw_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zt/2ztw_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Amino-acid biosynthesis]] | [[Category: Amino-acid biosynthesis]] | ||
[[Category: Branched-chain amino acid biosynthesis]] | [[Category: Branched-chain amino acid biosynthesis]] | ||
| + | [[Category: Cytoplasm]] | ||
[[Category: Decarboxylating dehydrogenase]] | [[Category: Decarboxylating dehydrogenase]] | ||
[[Category: Ipmdh]] | [[Category: Ipmdh]] | ||
Revision as of 06:50, 18 October 2018
Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+
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Categories: Flavobacterium thermophilum yoshida and oshima 1971 | 3-isopropylmalate dehydrogenase | Eguchi, T | Kumasaka, T | Nango, E | Amino-acid biosynthesis | Branched-chain amino acid biosynthesis | Cytoplasm | Decarboxylating dehydrogenase | Ipmdh | Leucine biosynthesis | Magnesium | Manganese | Metal-binding | Nad | Oxidoreductase
