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.
3pnv
From Proteopedia
(Difference between revisions)
m (Protected "3pnv" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | + | {{STRUCTURE_3pnv| PDB=3pnv | SCENE= }} | |
| + | ===V369M mutant of Glutamyl-tRNA synthetase from Mycobacterium tuberculosis=== | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/SYE_MYCTU SYE_MYCTU]] 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) (By similarity). | ||
| - | + | ==About this Structure== | |
| - | + | [[3pnv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PNV OCA]. | |
| - | + | [[Category: Glutamate--tRNA ligase]] | |
| + | [[Category: Mycobacterium tuberculosis]] | ||
| + | [[Category: Bartunik, H D.]] | ||
| + | [[Category: Kachalova, G S.]] | ||
| + | [[Category: Laurinavichiute, D.]] | ||
| + | [[Category: Atp-binding]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Non-discriminating glutamyl-trna aminoacylation]] | ||
| + | [[Category: Nucleotide-binding]] | ||
Revision as of 08:32, 8 May 2013
V369M mutant of Glutamyl-tRNA synthetase from Mycobacterium tuberculosis
Function
[SYE_MYCTU] 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) (By similarity).
About this Structure
3pnv is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
