2cv1
From Proteopedia
(Difference between revisions)
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<StructureSection load='2cv1' size='340' side='right'caption='[[2cv1]], [[Resolution|resolution]] 2.41Å' scene=''> | <StructureSection load='2cv1' size='340' side='right'caption='[[2cv1]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2cv1]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2cv1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CV1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GAU:(4S)-4-AMINO-5-HYDROXYPENTANOIC+ACID'>GAU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GAU:(4S)-4-AMINO-5-HYDROXYPENTANOIC+ACID'>GAU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g59|1g59]], [[1j09|1j09]], [[1n75|1n75]], [[1n77|1n77]], [[1n78|1n78]], [[2cuz|2cuz]], [[2cv0|2cv0]], [[2cv2|2cv2]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g59|1g59]], [[1j09|1j09]], [[1n75|1n75]], [[1n77|1n77]], [[1n78|1n78]], [[2cuz|2cuz]], [[2cv0|2cv0]], [[2cv2|2cv2]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cv1 OCA], [https://pdbe.org/2cv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cv1 RCSB], [https://www.ebi.ac.uk/pdbsum/2cv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cv1 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cv1 TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/SYE_THET8 SYE_THET8]] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).<ref>PMID:11224561</ref> <ref>PMID:17161369</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:01, 1 December 2021
Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu), ATP, and an analog of L-glutamate: a quaternary complex
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