1G59: Glutamyl-tRNA synthetase

Glutamyl-tRNA synthetase complexed with trna(glu). Determined by X-ray diffraction at 2.4 Å resolution. Released 1 Sept 2001.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Thermus thermophilus
Chains
4
Atoms
11,092
Mol. weight
156.17 kDa
Released
1 Sept 2001

Explore 1G59 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G59 contains 63 α-helices and 40 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 32 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand3-641
β-strand1512
α-helix16-3116
β-strand35-3841
β-strand4013
α-helix52-6211
β-strand6911
β-strand8113
α-helix82-854
α-helix86-9712
β-strand102-10544
α-helix109-11810
α-helix125-1284
α-helix131-1399
β-strand145-14844
β-strand155-16065
β-strand164-16965
α-helix170-1723
β-strand177-17934
β-strand18514
α-helix187-19711
β-strand202-20655
α-helix207-2093
α-helix213-22210
α-helix227-2282
β-strand229-23355
α-helix234-2363
β-strand23716
β-strand24316
β-strand25212
α-helix253-2586
α-helix263-27210
β-strand27517
α-helix286-2927
α-helix295-2973
β-strand29817
α-helix302-3032
β-strand30416
α-helix3051
α-helix307-31610
α-helix317-3215
α-helix324-33714
α-helix345-35511
α-helix356-3583
α-helix364-3685
α-helix370-3723
α-helix381-39515
α-helix398-4036
α-helix409-42214
α-helix428-43811
α-helix447-4548
α-helix456-46712
Chain C: 31 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand3-648
β-strand1519
α-helix16-3116
β-strand35-3848
β-strand40110
α-helix45-473
α-helix53-6210
β-strand6918
β-strand81110
α-helix86-9712
β-strand102-105411
α-helix109-11810
α-helix125-1284
α-helix131-1399
β-strand145-148411
β-strand155-160612
β-strand164-169612
α-helix170-1723
β-strand177-179311
β-strand185111
α-helix187-19711
β-strand202-206512
α-helix207-2093
α-helix213-22210
β-strand229-233512
α-helix234-2363
β-strand237113
β-strand243113
β-strand25219
α-helix253-2586
α-helix263-27210
β-strand275114
α-helix286-2927
α-helix295-2973
β-strand298114
α-helix302-3032
β-strand304113
α-helix3051
α-helix307-31610
α-helix317-3215
α-helix324-33714
α-helix345-35511
α-helix356-3583
α-helix364-3685
α-helix370-3723
α-helix381-39515
α-helix398-4036
α-helix409-42214
α-helix427-43812
α-helix447-4548
α-helix456-46712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Trna(glu)B, DRNA75
Glutamyl-tRNA synthetaseA, Cprotein468Thermus thermophilusP27000 (AlphaFold model)
Sequence of entity 1 (B, D), FASTA
>1G59_1 TRNA(GLU) (chains B, D)
GGCCCCAUCGUCUAGCGGUUAGGACGCGGCCCUCUCAAGGCCGAAACGGGGGUUCGAUUC
CCCCUGGGGUCACCA
Sequence of entity 2 (A, C), FASTA
>1G59_2 GLUTAMYL-TRNA SYNTHETASE (chains A, C)
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL
KWLGLSYDEGPDVAAPTGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG
GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK
SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD
KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD
TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA
AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA

Primary citation

Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase. Sekine, S., Nureki, O., Shimada, A. et al. Nat Struct Biol (2001) 8:203-206. DOI 10.1038/84927 · PubMed

Other PDB entries of the same protein (UniProt P27000 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1G59 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.