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2eg5
From Proteopedia
(Difference between revisions)
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<StructureSection load='2eg5' size='340' side='right' caption='[[2eg5]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2eg5' size='340' side='right' caption='[[2eg5]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2eg5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2eg5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cofca Cofca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EG5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EG5 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=XTS:9-[(2R,3R,4S,5R)-3,4-DIHYDROXY-5-(HYDROXYMETHYL)OXOLAN-2-YL]-3H-PURINE-2,6-DIONE'>XTS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=XTS:9-[(2R,3R,4S,5R)-3,4-DIHYDROXY-5-(HYDROXYMETHYL)OXOLAN-2-YL]-3H-PURINE-2,6-DIONE'>XTS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2efj|2efj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2efj|2efj]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=49390 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=49390 COFCA])</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=2eg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eg5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2eg5 RCSB], [http://www.ebi.ac.uk/pdbsum/2eg5 PDBsum]</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=2eg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eg5 OCA], [http://pdbe.org/2eg5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eg5 RCSB], [http://www.ebi.ac.uk/pdbsum/2eg5 PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/XMT1_COFCA XMT1_COFCA]] Involved in the biosynthesis of caffeine. Specific for xanthosine. Cannot use xanthosine 5'-monophosphate (XMP) as substrate. Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled. Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N-methylation activity. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2eg5" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Cofca]] |
[[Category: McCarthy, A A]] | [[Category: McCarthy, A A]] | ||
[[Category: McCarthy, J G]] | [[Category: McCarthy, J G]] | ||
Revision as of 22:43, 9 September 2015
The structure of xanthosine methyltransferase
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