4xeo: Difference between revisions
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New page: '''Unreleased structure''' The entry 4xeo is ON HOLD Authors: Zhou, H., Yang, X.L. Description: Crystal Structure of human AlaRS catalytic domain with R329H mutation [[Category: Unrele... |
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The entry | ==Crystal Structure of human AlaRS catalytic domain with R329H mutation== | ||
<StructureSection load='4xeo' size='340' side='right'caption='[[4xeo]], [[Resolution|resolution]] 1.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xeo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4XEO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xeo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xeo OCA], [https://pdbe.org/4xeo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xeo RCSB], [https://www.ebi.ac.uk/pdbsum/4xeo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xeo ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://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 == | |||
[https://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] | |||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Yang | [[Category: Large Structures]] | ||
[[Category: He W]] | |||
[[Category: Yang XL]] | |||
[[Category: Zhou H]] | |||
Latest revision as of 07:44, 27 September 2023
Crystal Structure of human AlaRS catalytic domain with R329H mutation
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