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2wfa
From Proteopedia
(Difference between revisions)
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==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.== | ==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.== | ||
<StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WFA FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z4o|1z4o]], [[2wf5|2wf5]], [[1o03|1o03]], [[1zol|1zol]], [[1z4n|1z4n]], [[1lvh|1lvh]], [[1o08|1o08]], [[2wf6|2wf6]], [[2wf8|2wf8]], [[2wf7|2wf7]], [[2wf9|2wf9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z4o|1z4o]], [[2wf5|2wf5]], [[1o03|1o03]], [[1zol|1zol]], [[1z4n|1z4n]], [[1lvh|1lvh]], [[1o08|1o08]], [[2wf6|2wf6]], [[2wf8|2wf8]], [[2wf7|2wf7]], [[2wf9|2wf9]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum]</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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://pdbe.org/2wfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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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=2wfa ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2wfa" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacterium lactis lister 1873]] | ||
[[Category: Beta-phosphoglucomutase]] | [[Category: Beta-phosphoglucomutase]] | ||
| - | [[Category: Lactococcus lactis]] | ||
[[Category: Alizadeh, T]] | [[Category: Alizadeh, T]] | ||
[[Category: Baxter, N J]] | [[Category: Baxter, N J]] | ||
Revision as of 11:43, 5 August 2016
Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.
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Categories: Bacterium lactis lister 1873 | Beta-phosphoglucomutase | Alizadeh, T | Baxter, N J | Bermel, W | Blackburn, G M | Bowler, M W | Cliff, M J | Hollfelder, F | Hounslow, A M | Pollard, S | Waltho, J P | Webster, C E | Williams, N H | Haloacid dehalogenase superfamily | Isomerase | Phosphotransferase | Transition state analogue
