This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3emk
From Proteopedia
(Difference between revisions)
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:3emk.jpg|left|200px]] | ||
| - | + | ==2.5A crystal structure of glucose/ribitol dehydrogenase from brucella melitensis== | |
| - | + | <StructureSection load='3emk' size='340' side='right'caption='[[3emk]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3emk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_melitensis Brucella melitensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EMK 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]] 2.5Å</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=3emk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emk OCA], [https://pdbe.org/3emk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3emk RCSB], [https://www.ebi.ac.uk/pdbsum/3emk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3emk ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q2YMG6_BRUA2 Q2YMG6_BRUA2] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[RuleBase:RU366074] | |
| - | + | == 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/em/3emk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3emk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Brucella melitensis]] | [[Category: Brucella melitensis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
2.5A crystal structure of glucose/ribitol dehydrogenase from brucella melitensis
| |||||||||||
