1vqv: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex Aeolicus== | ==Crystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex Aeolicus== | ||
<StructureSection load='1vqv' size='340' side='right'caption='[[1vqv]]' scene=''> | <StructureSection load='1vqv' size='340' side='right'caption='[[1vqv]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yaw 1yaw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQV FirstGlance]. <br> | <table><tr><td colspan='2'>[[1vqv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1yaw 1yaw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQV FirstGlance]. <br> | ||
</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=1vqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqv OCA], [https://pdbe.org/1vqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vqv RCSB], [https://www.ebi.ac.uk/pdbsum/1vqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vqv ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1vqv TOPSAN]</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]] 2.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1vqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqv OCA], [https://pdbe.org/1vqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vqv RCSB], [https://www.ebi.ac.uk/pdbsum/1vqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vqv ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1vqv TOPSAN]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/THIL_AQUAE THIL_AQUAE] Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.<ref>PMID:18311927</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 16: | Line 20: | ||
</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=1vqv ConSurf]. | </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=1vqv ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aquifex aeolicus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Burley SK]] | [[Category: Burley SK]] | ||
[[Category: Eswaramoorthy S]] | [[Category: Eswaramoorthy S]] | ||
[[Category: Swaminathan S]] | [[Category: Swaminathan S]] | ||
Latest revision as of 03:05, 28 December 2023
Crystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex AeolicusCrystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex Aeolicus
Structural highlights
FunctionTHIL_AQUAE Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
|
| ||||||||||||||||||