1vqv
From Proteopedia
(Difference between revisions)
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<StructureSection load='1vqv' size='340' side='right' caption='[[1vqv]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='1vqv' size='340' side='right' caption='[[1vqv]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1vqv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1vqv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VQV FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiamine-phosphate_kinase Thiamine-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.16 2.7.4.16] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiamine-phosphate_kinase Thiamine-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.16 2.7.4.16] </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=1vqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vqv RCSB], [http://www.ebi.ac.uk/pdbsum/1vqv PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1vqv TOPSAN]</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=1vqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vqv OCA], [http://pdbe.org/1vqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vqv RCSB], [http://www.ebi.ac.uk/pdbsum/1vqv PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1vqv TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://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]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aquifex aeolicus]] | + | [[Category: Aquifex aeolicus huber and stetter 2001]] |
[[Category: Thiamine-phosphate kinase]] | [[Category: Thiamine-phosphate kinase]] | ||
[[Category: Burley, S K]] | [[Category: Burley, S K]] | ||
Revision as of 00:43, 10 September 2015
Crystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex Aeolicus
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Categories: Aquifex aeolicus huber and stetter 2001 | Thiamine-phosphate kinase | Burley, S K | Eswaramoorthy, S | Structural genomic | Swaminathan, S | Dimer | Kinase | NYSGXRC, New York SGX Research Center for Structural Genomics | Phosphate | PSI, Protein structure initiative | T1881 | Thil | Transferase
