5axd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:06, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='5axd' size='340' side='right'caption='[[5axd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5axd' size='340' side='right'caption='[[5axd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5axd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AXD FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5axd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AXD FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=RBV:1-(BETA-D-RIBOFURANOSYL)-1H-1,2,4-TRIAZOLE-3-CARBOXAMIDE'>RBV</scene></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]] 1.6&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5axa|5axa]], [[5axb|5axb]], [[5axc|5axc]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=RBV:1-(BETA-D-RIBOFURANOSYL)-1H-1,2,4-TRIAZOLE-3-CARBOXAMIDE'>RBV</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ahcy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5axd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5axd OCA], [https://pdbe.org/5axd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5axd RCSB], [https://www.ebi.ac.uk/pdbsum/5axd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5axd ProSAT]</span></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=5axd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5axd OCA], [http://pdbe.org/5axd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5axd RCSB], [http://www.ebi.ac.uk/pdbsum/5axd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5axd ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== 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.
+
[https://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__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Adenosylhomocysteinase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Mus musculus]]
-
[[Category: Ishihara, M]]
+
[[Category: Ishihara M]]
-
[[Category: Kusakabe, Y]]
+
[[Category: Kusakabe Y]]
-
[[Category: Tanaka, N]]
+
[[Category: Tanaka N]]
-
[[Category: Hydrolase]]
+
-
[[Category: Hydrolase nucleoside complex]]
+

Current revision

Crystal structure of mouse SAHH complexed with ribavirin

PDB ID 5axd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools