2vd3
From Proteopedia
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| - | {{Structure | ||
| - | |PDB= 2vd3 |SIZE=350|CAPTION= <scene name='initialview01'>2vd3</scene> | ||
| - | |SITE= | ||
| - | |LIGAND= | ||
| - | |ACTIVITY= | ||
| - | |GENE= | ||
| - | |DOMAIN= | ||
| - | |RELATEDENTRY= | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd3 OCA], [http://www.ebi.ac.uk/pdbsum/2vd3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vd3 RCSB]</span> | ||
| - | }} | ||
| - | '''''' | + | ==The structure of histidine inhibited HisG from Methanobacterium thermoautotrophicum== |
| + | <StructureSection load='2vd3' size='340' side='right'caption='[[2vd3]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2vd3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VD3 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]] 2.45Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=2vd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd3 OCA], [https://pdbe.org/2vd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vd3 RCSB], [https://www.ebi.ac.uk/pdbsum/2vd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vd3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HIS1_METTH HIS1_METTH] 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/2vd3_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=2vd3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | == | + | *[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| + | [[Category: Methanothermobacter thermautotrophicus str. Delta H]] | ||
| + | [[Category: Lapthorn AJ]] | ||
| + | [[Category: Lohkamp B]] | ||
| + | [[Category: Schweikert T]] | ||
Current revision
The structure of histidine inhibited HisG from Methanobacterium thermoautotrophicum
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