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3hdo
From Proteopedia
(Difference between revisions)
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<StructureSection load='3hdo' size='340' side='right' caption='[[3hdo]], [[Resolution|resolution]] 1.61Å' scene=''> | <StructureSection load='3hdo' size='340' side='right' caption='[[3hdo]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hdo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3hdo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Geomg Geomg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HDO 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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </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=MG:MAGNESIUM+ION'>MG</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">hisC, Gmet_0385 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269799 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisC, Gmet_0385 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269799 GEOMG])</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=3hdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hdo RCSB], [http://www.ebi.ac.uk/pdbsum/3hdo PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/3hdo 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=3hdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hdo OCA], [http://pdbe.org/3hdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hdo RCSB], [http://www.ebi.ac.uk/pdbsum/3hdo PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/3hdo TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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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=3hdo ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminotransferase|Aminotransferase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Geomg]] |
[[Category: Histidinol-phosphate transaminase]] | [[Category: Histidinol-phosphate transaminase]] | ||
[[Category: Burley, S K]] | [[Category: Burley, S K]] | ||
Revision as of 02:56, 9 February 2016
Crystal Structure of a Histidinol-phosphate aminotransferase from Geobacter metallireducens
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Categories: Geomg | Histidinol-phosphate transaminase | Burley, S K | Damodharan, L | Structural genomic | Swaminathan, S | Amino-acid biosynthesis | Aminotransferase | Histidine biosynthesis | Histidinol-phosphate aminotransferase | NYSGXRC, New York SGX Research Center for Structural Genomics | PSI, Protein structure initiative | Pyridoxal phosphate | Transferase
