This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3g98

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal Structure of the C-Ala domain from Aquifex aeolicus alanyl-tRNA synthetase==
==Crystal Structure of the C-Ala domain from Aquifex aeolicus alanyl-tRNA synthetase==
-
<StructureSection load='3g98' size='340' side='right' caption='[[3g98]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+
<StructureSection load='3g98' size='340' side='right'caption='[[3g98]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3g98]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G98 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3g98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G98 FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr>
+
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alaS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alanine--tRNA_ligase Alanine--tRNA ligase], with EC number [https://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=3g98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g98 OCA], [http://pdbe.org/3g98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g98 RCSB], [http://www.ebi.ac.uk/pdbsum/3g98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g98 ProSAT]</span></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=3g98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g98 OCA], [https://pdbe.org/3g98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g98 RCSB], [https://www.ebi.ac.uk/pdbsum/3g98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g98 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/SYA_AQUAE SYA_AQUAE]] 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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (By similarity).[HAMAP-Rule:MF_00036]
+
[[https://www.uniprot.org/uniprot/SYA_AQUAE SYA_AQUAE]] 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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (By similarity).[HAMAP-Rule:MF_00036]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 31: Line 31:
==See Also==
==See Also==
-
*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
+
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 38: Line 38:
[[Category: Aquifex aeolicus huber and stetter 2001]]
[[Category: Aquifex aeolicus huber and stetter 2001]]
[[Category: Alanine--tRNA ligase]]
[[Category: Alanine--tRNA ligase]]
 +
[[Category: Large Structures]]
[[Category: Guo, M]]
[[Category: Guo, M]]
[[Category: Schimmel, P]]
[[Category: Schimmel, P]]

Revision as of 07:58, 9 March 2022

Crystal Structure of the C-Ala domain from Aquifex aeolicus alanyl-tRNA synthetase

PDB ID 3g98

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools