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==Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3==
==Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3==
<StructureSection load='2d7j' size='340' side='right' caption='[[2d7j]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
<StructureSection load='2d7j' size='340' side='right'caption='[[2d7j]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2d7j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrho Pyrho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D7J FirstGlance]. <br>
<table><tr><td colspan='2'>[[2d7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D7J FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] </span></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]] 1.89&#8491;</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=2d7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7j OCA], [http://pdbe.org/2d7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d7j RCSB], [http://www.ebi.ac.uk/pdbsum/2d7j PDBsum]</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=2d7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7j OCA], [https://pdbe.org/2d7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d7j RCSB], [https://www.ebi.ac.uk/pdbsum/2d7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d7j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GUAAA_PYRHO GUAAA_PYRHO]] Catalyzes the synthesis of GMP from XMP (By similarity).  
[https://www.uniprot.org/uniprot/GUAAA_PYRHO GUAAA_PYRHO] Catalyzes the synthesis of GMP from XMP (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d7/2d7j_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d7/2d7j_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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=2d7j ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrho]]
[[Category: Large Structures]]
[[Category: Kamo, M]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Kudo, N]]
[[Category: Kamo M]]
[[Category: Lee, W C]]
[[Category: Kudo N]]
[[Category: Maruoka, S]]
[[Category: Lee WC]]
[[Category: Nagata, K]]
[[Category: Maruoka S]]
[[Category: Tanokura, M]]
[[Category: Nagata K]]
[[Category: Alpha-beta-alpha]]
[[Category: Tanokura M]]
[[Category: Ligase]]

Latest revision as of 16:47, 13 March 2024

Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3

Structural highlights

2d7j is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.89Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUAAA_PYRHO Catalyzes the synthesis of GMP from XMP (By similarity).

Evolutionary Conservation

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

See Also

2d7j, resolution 1.89Å

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