2oo7: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="2oo7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oo7" /> ''''''<br /> ==About this Structure== is a [h... |
No edit summary |
||
| (18 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Crystal structure of a thermostable mutant of Bacillus subtilis Adenylate Kinase (T179I/Q199R)== | ||
<StructureSection load='2oo7' size='340' side='right'caption='[[2oo7]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
[[ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2oo7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OO7 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2oo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oo7 OCA], [https://pdbe.org/2oo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oo7 RCSB], [https://www.ebi.ac.uk/pdbsum/2oo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oo7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KAD_BACSU KAD_BACSU] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth. | |||
== 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/oo/2oo7_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=2oo7 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | |||
[[Category: Counago R]] | |||
[[Category: Myers JC]] | |||
[[Category: Shamoo Y]] | |||
[[Category: Wilson CJ]] | |||
[[Category: Wittung-Stafshede P]] | |||
[[Category: Wu G]] | |||
Latest revision as of 13:45, 30 August 2023
Crystal structure of a thermostable mutant of Bacillus subtilis Adenylate Kinase (T179I/Q199R)Crystal structure of a thermostable mutant of Bacillus subtilis Adenylate Kinase (T179I/Q199R)
Structural highlights
FunctionKAD_BACSU Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
| ||||||||||||||||||