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2vp2
From Proteopedia
(Difference between revisions)
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<StructureSection load='2vp2' size='340' side='right'caption='[[2vp2]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2vp2' size='340' side='right'caption='[[2vp2]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vp2]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2vp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VP2 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j90|1j90]], [[1zmx|1zmx]], [[2jcs|2jcs]], [[1oe0|1oe0]], [[1ot3|1ot3]], [[1zm7|1zm7]], [[2vp0|2vp0]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j90|1j90]], [[1zmx|1zmx]], [[2jcs|2jcs]], [[1oe0|1oe0]], [[1ot3|1ot3]], [[1zm7|1zm7]], [[2vp0|2vp0]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Deoxynucleoside_kinase Deoxynucleoside kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.145 2.7.1.145] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vp2 OCA], [https://pdbe.org/2vp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vp2 RCSB], [https://www.ebi.ac.uk/pdbsum/2vp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vp2 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DNK_DROME DNK_DROME]] Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, deoxyadenosine, deoxycytidine and deoxyguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated.<ref>PMID:10446143</ref> <ref>PMID:10692477</ref> <ref>PMID:16008571</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 2vp2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2vp2" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Thymidine kinase|Thymidine kinase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:42, 30 March 2022
Structural Studies of Nucleoside Analog and Feedback Inhibitor Binding to Drosophila Melanogaster Multisubstrate Deoxyribonucleoside Kinase
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Categories: Deoxynucleoside kinase | Drome | Large Structures | Eklund, H | Mikkelsen, N E | Munch-Petersen, B | Atp-binding | Complex | Deoxyribonucleoside kinase | Dna synthesis | Drosophila | Dttp | Feedback inhibition | Kinase | Nucleotide-binding | Phosphoprotein | Salvage pathway | Transferase

