4xeo
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==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. 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> | |
| - | + | </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> | |
| - | + | <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> | |
| - | [[ | + | </table> |
| - | [[ | + | == Disease == |
| - | [[Category: | + | [[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: He, W]] | ||
| + | [[Category: Yang, X L]] | ||
| + | [[Category: Zhou, H]] | ||
| + | [[Category: Cmt]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Trna synthetase]] | ||
Revision as of 19:34, 30 December 2015
Crystal Structure of human AlaRS catalytic domain with R329H mutation
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Categories: Alanine--tRNA ligase | He, W | Yang, X L | Zhou, H | Cmt | Ligase | Trna synthetase
