2hsz
From Proteopedia
(Difference between revisions)
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<StructureSection load='2hsz' size='340' side='right'caption='[[2hsz]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2hsz' size='340' side='right'caption='[[2hsz]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2hsz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2hsz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Histophilus_somni_129PT Histophilus somni 129PT]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HSZ 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]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2hsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsz OCA], [https://pdbe.org/2hsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsz RCSB], [https://www.ebi.ac.uk/pdbsum/2hsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsz ProSAT], [https://www.topsan.org/Proteins/JCSG/2hsz TOPSAN]</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=2hsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsz OCA], [https://pdbe.org/2hsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsz RCSB], [https://www.ebi.ac.uk/pdbsum/2hsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsz ProSAT], [https://www.topsan.org/Proteins/JCSG/2hsz TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q0I1W8_HISS1 Q0I1W8_HISS1] Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.[HAMAP-Rule:MF_00495] | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hs/2hsz_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hs/2hsz_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Histophilus somni 129PT]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Hydrolase]] | ||
| - | [[Category: Jcsg]] | ||
| - | [[Category: PSI, Protein structure initiative]] | ||
Current revision
Crystal structure of a predicted phosphoglycolate phosphatase (hs_0176) from haemophilus somnus 129pt at 1.90 A resolution
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