3hdo: Difference between revisions

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==Crystal Structure of a Histidinol-phosphate aminotransferase from Geobacter metallireducens==
==Crystal Structure of a Histidinol-phosphate aminotransferase from Geobacter metallireducens==
<StructureSection load='3hdo' size='340' side='right' caption='[[3hdo]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
<StructureSection load='3hdo' size='340' side='right'caption='[[3hdo]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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 GEOMG])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hdo OCA], [https://pdbe.org/3hdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hdo RCSB], [https://www.ebi.ac.uk/pdbsum/3hdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hdo ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/3hdo TOPSAN]</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://pdbe.org/3hdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hdo RCSB], [http://www.ebi.ac.uk/pdbsum/3hdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hdo ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/3hdo TOPSAN]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/3hdo_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/3hdo_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Aminotransferase|Aminotransferase]]
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Geomg]]
[[Category: Large Structures]]
[[Category: Histidinol-phosphate transaminase]]
[[Category: Burley SK]]
[[Category: Burley, S K]]
[[Category: Damodharan L]]
[[Category: Damodharan, L]]
[[Category: Swaminathan S]]
[[Category: Structural genomic]]
[[Category: Swaminathan, S]]
[[Category: Amino-acid biosynthesis]]
[[Category: Aminotransferase]]
[[Category: Histidine biosynthesis]]
[[Category: Histidinol-phosphate aminotransferase]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: PSI, Protein structure initiative]]
[[Category: Pyridoxal phosphate]]
[[Category: Transferase]]

Latest revision as of 09:17, 27 November 2024

Crystal Structure of a Histidinol-phosphate aminotransferase from Geobacter metallireducensCrystal Structure of a Histidinol-phosphate aminotransferase from Geobacter metallireducens

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.61Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3hdo, resolution 1.61Å

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