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1xjg
From Proteopedia
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==Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex== | ==Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex== | ||
| - | <StructureSection load='1xjg' size='340' side='right' caption='[[1xjg]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='1xjg' size='340' side='right'caption='[[1xjg]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1xjg]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1xjg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XJG 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]] 2.5Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjg OCA], [https://pdbe.org/1xjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xjg RCSB], [https://www.ebi.ac.uk/pdbsum/1xjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjg ProSAT]</span></td></tr> |
| - | < | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O33839_THEMT O33839_THEMT] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xj/1xjg_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xj/1xjg_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Ribonucleotide reductase|Ribonucleotide reductase]] | *[[Ribonucleotide reductase|Ribonucleotide reductase]] | ||
| + | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Eliasson | + | [[Category: Eliasson R]] |
| - | [[Category: Jordan | + | [[Category: Jordan A]] |
| - | [[Category: Larsson | + | [[Category: Larsson K-M]] |
| - | [[Category: Logan | + | [[Category: Logan DT]] |
| - | [[Category: Nordlund | + | [[Category: Nordlund P]] |
| - | [[Category: Reichard | + | [[Category: Reichard P]] |
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Current revision
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex
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