3nas: Difference between revisions

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'''Unreleased structure'''


The entry 3nas is ON HOLD
==The crystal structure of beta-phosphoglucomutase from Bacillus subtilis==
<StructureSection load='3nas' size='340' side='right'caption='[[3nas]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nas]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NAS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=3nas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nas OCA], [https://pdbe.org/3nas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nas RCSB], [https://www.ebi.ac.uk/pdbsum/3nas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nas ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGMB_BACSU PGMB_BACSU] Catalyze the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. It play a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/na/3nas_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=3nas ConSurf].
<div style="clear:both"></div>


Authors: Zhang, Z., Burley, S.K., Swaminathan, S., New York SGX Research Center for Structural Genomics (NYSGXRC)
==See Also==
 
*[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]]
Description: The crystal structure of beta-phosphoglucomutase from Bacillus subtilis (CASP Target)
__TOC__
 
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 16 08:29:41 2010''
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Burley SK]]
[[Category: Swaminathan S]]
[[Category: Zhang Z]]

Latest revision as of 05:09, 21 November 2024

The crystal structure of beta-phosphoglucomutase from Bacillus subtilisThe crystal structure of beta-phosphoglucomutase from Bacillus subtilis

Structural highlights

3nas is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PGMB_BACSU Catalyze the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. It play a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose (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

3nas, resolution 3.00Å

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