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2hg8
From Proteopedia
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==Crystal Structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase complexed with its substrate mimic, N-methyl leucine.== | ==Crystal Structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase complexed with its substrate mimic, N-methyl leucine.== | ||
<StructureSection load='2hg8' size='340' side='right' caption='[[2hg8]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2hg8' size='340' side='right' caption='[[2hg8]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=2hg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hg8 OCA], [http://pdbe.org/2hg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hg8 RCSB], [http://www.ebi.ac.uk/pdbsum/2hg8 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=2hg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hg8 OCA], [http://pdbe.org/2hg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hg8 RCSB], [http://www.ebi.ac.uk/pdbsum/2hg8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hg8 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hg8 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2hg8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2hg8" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Aminotransferase|Aminotransferase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 08:11, 18 October 2017
Crystal Structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase complexed with its substrate mimic, N-methyl leucine.
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