2vd2: Difference between revisions
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==The crystal structure of HisG from B. subtilis== | |||
<StructureSection load='2vd2' size='340' side='right'caption='[[2vd2]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
=== | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vd2]] is a 1 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=2VD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VD2 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]] 2.85Å</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=2vd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd2 OCA], [https://pdbe.org/2vd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vd2 RCSB], [https://www.ebi.ac.uk/pdbsum/2vd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vd2 ProSAT]</span></td></tr> | ||
[[2vd2]] is a 1 chain structure | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HIS1_BACSU HIS1_BACSU] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). | |||
== 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/vd/2vd2_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=2vd2 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[ATP | *[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lapthorn AJ]] | ||
[[Category: | [[Category: Lohkamp B]] | ||
[[Category: | [[Category: Riboldi-Tunniclife A]] | ||
Latest revision as of 12:57, 9 May 2024
The crystal structure of HisG from B. subtilisThe crystal structure of HisG from B. subtilis
Structural highlights
FunctionHIS1_BACSU Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). 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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