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==Crystal structure of enolase AGR_L_2751 from Agrobacterium Tumefaciens==
==Crystal structure of enolase AGR_L_2751 from Agrobacterium Tumefaciens==
<StructureSection load='1rvk' size='340' side='right' caption='[[1rvk]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1rvk' size='340' side='right'caption='[[1rvk]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1rvk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrfc Agrfc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RVK FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RVK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.7&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1rvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rvk OCA], [http://pdbe.org/1rvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rvk RCSB], [http://www.ebi.ac.uk/pdbsum/1rvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rvk ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1rvk TOPSAN]</span></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=1rvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rvk OCA], [https://pdbe.org/1rvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rvk RCSB], [https://www.ebi.ac.uk/pdbsum/1rvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rvk ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1rvk 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/rv/1rvk_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rv/1rvk_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>
</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=1rvk ConSurf].
</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=1rvk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Enolase 3D structures|Enolase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Agrfc]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Almo SC]]
[[Category: Burley, S K]]
[[Category: Burley SK]]
[[Category: Fedorov, A A]]
[[Category: Fedorov AA]]
[[Category: Fedorov, E V]]
[[Category: Fedorov EV]]
[[Category: Gerlt, J A]]
[[Category: Gerlt JA]]
[[Category: Millikin, C]]
[[Category: Millikin C]]
[[Category: Structural genomic]]
[[Category: Thirumuruhan R]]
[[Category: Thirumuruhan, R]]
[[Category: Zencheck W]]
[[Category: Zencheck, W]]
[[Category: Enolase superfamily]]
[[Category: Mr gi-17937161]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: PSI, Protein structure initiative]]
[[Category: Target t1522]]
[[Category: Unknown function]]

Latest revision as of 11:47, 6 November 2024

Crystal structure of enolase AGR_L_2751 from Agrobacterium TumefaciensCrystal structure of enolase AGR_L_2751 from Agrobacterium Tumefaciens

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
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

1rvk, resolution 1.70Å

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