1nj6: Difference between revisions
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< | ==Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to alanine sulfamoyl adenylate== | ||
<StructureSection load='1nj6' size='340' side='right'caption='[[1nj6]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nj6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NJ6 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]] 2.85Å</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1nj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nj6 OCA], [https://pdbe.org/1nj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nj6 RCSB], [https://www.ebi.ac.uk/pdbsum/1nj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nj6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SYP_METTH SYP_METTH] Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine.[HAMAP-Rule:MF_01571] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/1nj6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nj6 ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
__TOC__ | |||
== | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Methanothermobacter thermautotrophicus str. Delta H]] | |||
[[Category: Kamtekar S]] | |||
[[Category: Kennedy WD]] | |||
[[Category: Soll D]] | |||
[[Category: Stathopoulos C]] | |||
[[Category: Steitz TA]] | |||
[[Category: | [[Category: Wang J]] | ||
[[Category: | |||
[[Category: Kamtekar | |||
[[Category: Kennedy | |||
[[Category: Soll | |||
[[Category: Stathopoulos | |||
[[Category: Steitz | |||
[[Category: Wang | |||
Latest revision as of 10:57, 14 February 2024
Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to alanine sulfamoyl adenylateCrystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to alanine sulfamoyl adenylate
Structural highlights
FunctionSYP_METTH Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine.[HAMAP-Rule:MF_01571] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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