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== | |||
==Glucosamine-6-Phosphate Deaminase Complexed with the Allosteric Activator N-Acetyl-Glucoamine-6-Phosphate both in the Active and Allosteric sites.== | |||
<StructureSection load='2wu1' size='340' side='right' caption='[[2wu1]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2wu1' size='340' side='right' caption='[[2wu1]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fs5|1fs5]], [[1hot|1hot]], [[1fs6|1fs6]], [[1cd5|1cd5]], [[1frz|1frz]], [[1jt9|1jt9]], [[1fqo|1fqo]], [[1fsf|1fsf]], [[1hor|1hor]], [[1dea|1dea]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fs5|1fs5]], [[1hot|1hot]], [[1fs6|1fs6]], [[1cd5|1cd5]], [[1frz|1frz]], [[1jt9|1jt9]], [[1fqo|1fqo]], [[1fsf|1fsf]], [[1hor|1hor]], [[1dea|1dea]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] </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=2wu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wu1 OCA], [http://pdbe.org/2wu1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wu1 RCSB], [http://www.ebi.ac.uk/pdbsum/2wu1 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=2wu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wu1 OCA], [http://pdbe.org/2wu1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wu1 RCSB], [http://www.ebi.ac.uk/pdbsum/2wu1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wu1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/2wu1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/2wu1_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> | ||
Revision as of 12:08, 26 September 2018
Glucosamine-6-Phosphate Deaminase Complexed with the Allosteric Activator N-Acetyl-Glucoamine-6-Phosphate both in the Active and Allosteric sites.Glucosamine-6-Phosphate Deaminase Complexed with the Allosteric Activator N-Acetyl-Glucoamine-6-Phosphate both in the Active and Allosteric sites.
Structural highlights
Function[NAGB_ECOLI] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.[HAMAP-Rule:MF_01241] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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