3lv8: Difference between revisions
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< | ==1.8 Angstrom resolution crystal structure of a thymidylate kinase (tmk) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with TMP, thymidine-5'-diphosphate and ADP== | ||
<StructureSection load='3lv8' size='340' side='right' caption='[[3lv8]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3lv8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LV8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene>, <scene name='pdbligand=TYD:THYMIDINE-5-DIPHOSPHATE'>TYD</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n2i|3n2i]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmk, VC_2016 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lv8 OCA], [http://pdbe.org/3lv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lv8 RCSB], [http://www.ebi.ac.uk/pdbsum/3lv8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lv8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/KTHY_VIBCH KTHY_VIBCH]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (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/lv/3lv8_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=3lv8 ConSurf]. | |||
<div style="clear:both"></div> | |||
== | ==See Also== | ||
*[[Thymidylate kinase|Thymidylate kinase]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Vibch]] | |||
[[Category: | |||
[[Category: DTMP kinase]] | [[Category: DTMP kinase]] | ||
[[Category: Anderson, W F | [[Category: Anderson, W F]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Dubrovska, I | [[Category: Dubrovska, I]] | ||
[[Category: Halavaty, A S | [[Category: Halavaty, A S]] | ||
[[Category: Kwon, K | [[Category: Kwon, K]] | ||
[[Category: Minasov, G | [[Category: Minasov, G]] | ||
[[Category: Shuvalova, L | [[Category: Shuvalova, L]] | ||
[[Category: Winsor, J | [[Category: Winsor, J]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Csgid]] | [[Category: Csgid]] | ||
[[Category: Infectious disease]] | [[Category: Infectious disease]] | ||
| Line 32: | Line 43: | ||
[[Category: Nucleotide biosynthesis]] | [[Category: Nucleotide biosynthesis]] | ||
[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
[[Category: Thymidylate kinase]] | [[Category: Thymidylate kinase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
Latest revision as of 00:01, 5 August 2016
1.8 Angstrom resolution crystal structure of a thymidylate kinase (tmk) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with TMP, thymidine-5'-diphosphate and ADP1.8 Angstrom resolution crystal structure of a thymidylate kinase (tmk) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with TMP, thymidine-5'-diphosphate and ADP
Structural highlights
Function[KTHY_VIBCH] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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