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1og4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1og4' size='340' side='right' caption='[[1og4]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1og4' size='340' side='right' caption='[[1og4]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1og4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1og4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OG4 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gxy|1gxy]], [[1gxz|1gxz]], [[1gy0|1gy0]], [[1og1|1og1]], [[1og3|1og3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gxy|1gxy]], [[1gxz|1gxz]], [[1gy0|1gy0]], [[1og1|1og1]], [[1og3|1og3]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)--protein-arginine_ADP-ribosyltransferase NAD(+)--protein-arginine ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.31 2.4.2.31] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)--protein-arginine_ADP-ribosyltransferase NAD(+)--protein-arginine ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.31 2.4.2.31] </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=1og4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1og4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1og4 RCSB], [http://www.ebi.ac.uk/pdbsum/1og4 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=1og4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1og4 OCA], [http://pdbe.org/1og4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1og4 RCSB], [http://www.ebi.ac.uk/pdbsum/1og4 PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NAR2B_RAT NAR2B_RAT]] Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent). | ||
== 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 1og4" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Buffalo rat]] |
[[Category: Koch-Nolte, F]] | [[Category: Koch-Nolte, F]] | ||
[[Category: Marquez, V E]] | [[Category: Marquez, V E]] | ||
Revision as of 04:55, 10 September 2015
CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 MUTANT E189A IN COMPLEX WITH NADH
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