4xeo: Difference between revisions

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'''Unreleased structure'''
==Crystal Structure of human AlaRS catalytic domain with R329H mutation==
 
<StructureSection load='4xeo' size='340' side='right' caption='[[4xeo]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
The entry 4xeo is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4xeo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XEO FirstGlance]. <br>
Authors: Zhou, H., He, W., Yang, X.L.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A5A:5-O-(N-(L-ALANYL)-SULFAMOYL)ADENOSINE'>A5A</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine--tRNA_ligase Alanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.7 6.1.1.7] </span></td></tr>
Description: Crystal Structure of human AlaRS catalytic domain with R329H mutation
<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=4xeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xeo OCA], [http://pdbe.org/4xeo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xeo RCSB], [http://www.ebi.ac.uk/pdbsum/4xeo PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Autosomal dominant Charcot-Marie-Tooth disease type 2N. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.  
== Function ==
[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]
__TOC__
</StructureSection>
[[Category: Alanine--tRNA ligase]]
[[Category: He, W]]
[[Category: Yang, X L]]
[[Category: Zhou, H]]
[[Category: Zhou, H]]
[[Category: Yang, X.L]]
[[Category: Cmt]]
[[Category: He, W]]
[[Category: Ligase]]
[[Category: Trna synthetase]]