4rra

N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Thr3AA (snapshot 1)

spinqualitylabelsall models 4rra, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rra is a 1 chain structure with sequence from Aeropyrum pernix K1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: A3T, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SYTE_AERPE Freestanding tRNA editing subunit of threonine--tRNA ligase, the catalytic subunit is probably AC Q9YDW0. Deacylates (edits) mischarged L-seryl-tRNA(Thr) in trans; has no activity on correctly charged L-threonyl-tRNA(Thr) (PubMed:26113036). Probably does not aminoacylate tRNA(Thr) (By similarity). Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is catalyzed by the 2'-OH of A76 of tRNA(Thr) (PubMed:26113036).[UniProtKB:Q980D1]

Proteopedia Page Contributors and Editors (what is this?)

OCA