1GLN: Glutamyl-tRNA synthetase

Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Oct 1995.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Thermus thermophilus
Chains: 1
Atoms: 3,973
Mol. weight: 53.98 kDa
Released: 15 Oct 1995

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

Secondary structure: helices and β-sheets

1GLN contains 28 α-helices and 17 β-strands across 1 chain. 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: 28 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
β-strand	15	1	2
α-helix	16-30	15
β-strand	35-38	4	1
α-helix	52-62	11
β-strand	69	1	1
β-strand	70	1	3
α-helix	71-73	3
β-strand	74	1	3
α-helix	87-97	11
β-strand	102-105	4	4
α-helix	109-119	11
α-helix	125-128	4
α-helix	131-140	10
β-strand	145-148	4	4
β-strand	155-160	6	5
β-strand	164-169	6	5
β-strand	177-179	3	4
β-strand	185	1	4
α-helix	187-198	12
β-strand	202-206	5	6
α-helix	207-212	6
α-helix	213-222	10
β-strand	229-233	5	6
β-strand	237	1	7
β-strand	252	1	2
α-helix	253-258	6
α-helix	263-272	10
α-helix	286-289	4
α-helix	295-297	3
β-strand	304	1	7
α-helix	307-320	14
α-helix	324-330	7
α-helix	332-337	6
α-helix	345-355	11
α-helix	356-358	3
α-helix	362-364	3
α-helix	365-368	4
α-helix	370-372	3
α-helix	381-389	9
α-helix	391-403	13
α-helix	409-423	15
α-helix	428-439	12
α-helix	447-454	8
α-helix	456-467	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamyl-tRNA synthetase	A	protein	468	Thermus thermophilus	P27000 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GLN_1 GLUTAMYL-TRNA SYNTHETASE (chains A)
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL
KWLGLSYDEGPDVAAPTGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG
GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK
SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD
KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD
TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA
AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA

Primary citation

Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Nureki, O., Vassylyev, D.G., Katayanagi, K. et al. Science (1995) 267:1958-1965. PubMed

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

1J09 1.8 Å, Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP…
1N75 1.9 Å, Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP.
2CUZ 1.98 Å, Glutamyl-tRNA synthetase from Thermus thermophilus in complex with L-glutamate
1N78 2.1 Å, Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with…
2DXI 2.2 Å, 2.2 A crystal structure of glutamyl-tRNA synthetase from Thermus thermophilus complexed…
1G59 2.4 Å, Glutamyl-tRNA synthetase complexed with trna(glu).
1N77 2.4 Å, Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with…
2CV0 2.4 Å, Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and…
2CV1 2.41 Å, Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu), ATP, and…
2CV2 2.69 Å, Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and an…

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