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3euc
From Proteopedia
(Difference between revisions)
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<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=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3euc]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3euc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupnj Cupnj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EUC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YP_297314.1, hisC2, Reut_A3110 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YP_297314.1, hisC2, Reut_A3110 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264198 CUPNJ])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3euc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3euc OCA], [https://pdbe.org/3euc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3euc RCSB], [https://www.ebi.ac.uk/pdbsum/3euc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3euc ProSAT], [https://www.topsan.org/Proteins/JCSG/3euc TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 09:16, 23 February 2022
Crystal structure of histidinol-phosphate aminotransferase (YP_297314.1) from RALSTONIA EUTROPHA JMP134 at 2.05 A resolution
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Categories: Cupnj | Histidinol-phosphate transaminase | Large Structures | 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
