3pd4: Difference between revisions
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[[Image:3pd4.png|left|200px]] | |||
[[Image:3pd4. | |||
{{STRUCTURE_3pd4| PDB=3pd4 | SCENE= }} | {{STRUCTURE_3pd4| PDB=3pd4 | SCENE= }} | ||
===Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with glycyl-3'-aminoadenosine=== | ===Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with glycyl-3'-aminoadenosine=== | ||
{{ABSTRACT_PUBMED_21098258}} | {{ABSTRACT_PUBMED_21098258}} | ||
==About this Structure== | ==About this Structure== | ||
[[3pd4]] is a 2 chain structure of [[Aminoacyl tRNA Synthetase]] with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PD4 OCA]. | |||
==See Also== | |||
*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021098258</ref><references group="xtra"/> | ||
[[Category: Pyrococcus abyssi]] | [[Category: Pyrococcus abyssi]] | ||
[[Category: Threonine--tRNA ligase]] | [[Category: Threonine--tRNA ligase]] | ||
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[[Category: Ligase]] | [[Category: Ligase]] | ||
[[Category: Translation]] | [[Category: Translation]] | ||
Revision as of 20:00, 26 July 2012
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with glycyl-3'-aminoadenosineCrystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with glycyl-3'-aminoadenosine
Template:ABSTRACT PUBMED 21098258
About this StructureAbout this Structure
3pd4 is a 2 chain structure of Aminoacyl tRNA Synthetase with sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Hussain T, Kamarthapu V, Kruparani SP, Deshmukh MV, Sankaranarayanan R. Mechanistic insights into cognate substrate discrimination during proofreading in translation. Proc Natl Acad Sci U S A. 2010 Nov 22. PMID:21098258 doi:10.1073/pnas.1014299107