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3euc
From Proteopedia
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==Crystal structure of histidinol-phosphate aminotransferase (YP_297314.1) from RALSTONIA EUTROPHA JMP134 at 2.05 A resolution== | ==Crystal structure of histidinol-phosphate aminotransferase (YP_297314.1) from RALSTONIA EUTROPHA JMP134 at 2.05 A resolution== | ||
<StructureSection load='3euc' size='340' side='right' caption='[[3euc]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='3euc' size='340' side='right' caption='[[3euc]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YP_297314.1, hisC2, Reut_A3110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264198 CUPPJ])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YP_297314.1, hisC2, Reut_A3110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264198 CUPPJ])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </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=3euc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3euc OCA], [http://pdbe.org/3euc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3euc RCSB], [http://www.ebi.ac.uk/pdbsum/3euc PDBsum], [http://www.topsan.org/Proteins/JCSG/3euc TOPSAN]</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=3euc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3euc OCA], [http://pdbe.org/3euc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3euc RCSB], [http://www.ebi.ac.uk/pdbsum/3euc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3euc ProSAT], [http://www.topsan.org/Proteins/JCSG/3euc TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 09:19, 25 October 2017
Crystal structure of histidinol-phosphate aminotransferase (YP_297314.1) from RALSTONIA EUTROPHA JMP134 at 2.05 A resolution
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Categories: Cuppj | Histidinol-phosphate transaminase | Structural genomic | Amino-acid biosynthesis | Aminotransferase | Aminotransferase class i and ii | Histidine biosynthesis | Histidinol-phosphate aminotransferase | Jcsg | PSI, Protein structure initiative | Pyridoxal phosphate | Transferase | Yp 297314 1
