2vd2
From Proteopedia
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<StructureSection load='2vd2' size='340' side='right'caption='[[2vd2]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='2vd2' size='340' side='right'caption='[[2vd2]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </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> | <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> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Lapthorn | + | [[Category: Lapthorn AJ]] |
| - | [[Category: Lohkamp | + | [[Category: Lohkamp B]] |
| - | [[Category: Riboldi-Tunniclife | + | [[Category: Riboldi-Tunniclife A]] |
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Current revision
The crystal structure of HisG from B. subtilis
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