4cd6: Difference between revisions

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 <StructureSection load='4cd6' size='340' side='right'caption='[[4cd6]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4cd6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27009 Atcc 27009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CD6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4cd6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CD6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IFM:5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE'>IFM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IFM:5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE'>IFM</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cd4|4cd4]], [[4cd5|4cd5]], [[4cd7|4cd7]], [[4cd8|4cd8]]</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=4cd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd6 OCA], [https://pdbe.org/4cd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cd6 RCSB], [https://www.ebi.ac.uk/pdbsum/4cd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd6 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=4cd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd6 OCA], [http://pdbe.org/4cd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cd6 RCSB], [http://www.ebi.ac.uk/pdbsum/4cd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd6 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[[https://www.uniprot.org/uniprot/A5H1I6_9BACL A5H1I6_9BACL]]
-Mannosidases catalyze the hydrolysis of a diverse range of polysaccharides and glycoconjugates, and the various sequence-based mannosidase families have evolved ingenious strategies to overcome the stereoelectronic challenges of mannoside chemistry. Using a combination of computational chemistry, inhibitor design and synthesis, and X-ray crystallography of inhibitor/enzyme complexes, it is demonstrated that mannoimidazole-type inhibitors are energetically poised to report faithfully on mannosidase transition-state conformation, and provide direct evidence for the conformational itinerary used by diverse mannosidases, including beta-mannanases from families GH26 and GH113. Isofagomine-type inhibitors are poor mimics of transition-state conformation, owing to the high energy barriers that must be crossed to attain mechanistically relevant conformations, however, these sugar-shaped heterocycles allow the acquisition of ternary complexes that span the active site, thus providing valuable insight into active-site residues involved in substrate recognition.
-Combined inhibitor free-energy landscape and structural analysis reports on the mannosidase conformational coordinate.,Williams RJ, Iglesias-Fernandez J, Stepper J, Jackson A, Thompson AJ, Lowe EC, White JM, Gilbert HJ, Rovira C, Davies GJ, Williams SJ Angew Chem Int Ed Engl. 2014 Jan 20;53(4):1087-91. doi: 10.1002/anie.201308334., Epub 2013 Dec 11. PMID:24339341<ref>PMID:24339341</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4cd6" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 27009]]
+[[Category: Alicyclobacillus acidocaldarius]]
 [[Category: Large Structures]]
-[[Category: Mannan endo-1,4-beta-mannosidase]]
+[[Category: Davies GJ]]
-[[Category: Davies, G J]]
+[[Category: Gilbert HJ]]
-[[Category: Gilbert, H J]]
+[[Category: Iglesias-Fernandez J]]
-[[Category: Iglesias-Fernandez, J]]
+[[Category: Jackson A]]
-[[Category: Jackson, A]]
+[[Category: Lowe EC]]
-[[Category: Lowe, E C]]
+[[Category: Rovira C]]
-[[Category: Rovira, C]]
+[[Category: Stepper J]]
-[[Category: Stepper, J]]
+[[Category: Thompson AJ]]
-[[Category: Thompson, A J]]
+[[Category: White JM]]
-[[Category: White, J M]]
+[[Category: Williams RJ]]
-[[Category: Williams, R J]]
+[[Category: Williams SJ]]
-[[Category: Williams, S J]]
-[[Category: Beta-mannosidase]]
-[[Category: Biocatalysis]]
-[[Category: Cazy]]
-[[Category: Conformation]]
-[[Category: Enzyme-carbohydrate interaction]]
-[[Category: Gh113]]
-[[Category: Gh26]]
-[[Category: Glycosidase inhibition]]
-[[Category: Glycoside hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Mannosidase]]
-[[Category: Quantum mechanic]]