2fem
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2fem" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fem, resolution 1.90Å" /> '''Mutant R188M of the ...) |
|||
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2fem.gif|left|200px]]<br /><applet load="2fem" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2fem, resolution 1.90Å" /> | ||
| - | '''Mutant R188M of the Cytidine Monophosphate Kinase From E. Coli'''<br /> | ||
| - | == | + | ==Mutant R188M of the Cytidine Monophosphate Kinase From E. Coli== |
| - | + | <StructureSection load='2fem' size='340' side='right'caption='[[2fem]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2fem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEM 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]] 1.9Å</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=2fem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fem OCA], [https://pdbe.org/2fem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fem RCSB], [https://www.ebi.ac.uk/pdbsum/2fem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fem ProSAT]</span></td></tr> | |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | [[ | + | [https://www.uniprot.org/uniprot/KCY_ECOLI KCY_ECOLI] ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.<ref>PMID:8190075</ref> <ref>PMID:7836281</ref> |
| - | + | == 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/fe/2fem_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=2fem ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Cytidine monophosphate kinase|Cytidine monophosphate kinase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Alexov E]] | ||
| + | [[Category: Barzu O]] | ||
| + | [[Category: Bertrand T]] | ||
| + | [[Category: Briozzo P]] | ||
| + | [[Category: Bucurenci N]] | ||
| + | [[Category: Gilles AM]] | ||
| + | [[Category: Munier-Lehmann H]] | ||
| + | [[Category: Ofiteru A]] | ||
| + | [[Category: Tourneux L]] | ||
Current revision
Mutant R188M of the Cytidine Monophosphate Kinase From E. Coli
| |||||||||||

