5axa
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of mouse SAHH complexed with adenosine== | |
| - | + | <StructureSection load='5axa' size='340' side='right' caption='[[5axa]], [[Resolution|resolution]] 1.55Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5axa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AXA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5axb|5axb]], [[5axc|5axc]], [[5axd|5axd]]</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=5axa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5axa OCA], [http://pdbe.org/5axa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5axa RCSB], [http://www.ebi.ac.uk/pdbsum/5axa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5axa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SAHH_MOUSE SAHH_MOUSE]] Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Adenosylhomocysteinase]] | ||
| + | [[Category: Ishihara, M]] | ||
| + | [[Category: Kusakabe, Y]] | ||
| + | [[Category: Tanaka, N]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase nucleoside complex]] | ||
Revision as of 15:33, 27 July 2016
Crystal structure of mouse SAHH complexed with adenosine
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