2cwk: Difference between revisions

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<StructureSection load='2cwk' size='340' side='right'caption='[[2cwk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='2cwk' size='340' side='right'caption='[[2cwk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cwk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CWK FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cwk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CWK FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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=2cwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwk OCA], [https://pdbe.org/2cwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cwk RCSB], [https://www.ebi.ac.uk/pdbsum/2cwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cwk ProSAT], [https://www.topsan.org/Proteins/RSGI/2cwk 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=2cwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwk OCA], [https://pdbe.org/2cwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cwk RCSB], [https://www.ebi.ac.uk/pdbsum/2cwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cwk ProSAT], [https://www.topsan.org/Proteins/RSGI/2cwk TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NDK_PYRHO NDK_PYRHO]] Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.  
[https://www.uniprot.org/uniprot/NDK_PYRHO NDK_PYRHO] Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Nucleoside-diphosphate kinase]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Pyrococcus horikoshii]]
[[Category: Kato-Murayama M]]
[[Category: Kato-Murayama, M]]
[[Category: Murayama K]]
[[Category: Murayama, K]]
[[Category: Shirouzu M]]
[[Category: Structural genomic]]
[[Category: Yokoyama S]]
[[Category: Shirouzu, M]]
[[Category: Yokoyama, S]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Rsgi]]
[[Category: Transferase]]

Latest revision as of 13:44, 13 March 2024

Crystal structure of nucleotide diphosphate kinase from Pyrococcus horikoshii

2cwk, resolution 1.75Å

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