2CV0: Glutamyl-tRNA synthetase

Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and L-glutamate. Determined by X-ray diffraction at 2.4 Å resolution. Released 5 Sept 2006.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Thermus thermophilus
Chains
4
Atoms
11,125
Mol. weight
156.53 kDa
Ligands
GLU, MG
Released
5 Sept 2006

Explore 2CV0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CV0 contains 63 α-helices and 42 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: 30 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand3-641
α-helix141
β-strand1512
α-helix16-3116
β-strand35-3841
β-strand4013
α-helix52-6312
β-strand6911
β-strand7014
β-strand7414
β-strand8113
α-helix82-854
α-helix86-9914
β-strand102-10545
α-helix109-11911
α-helix125-1284
α-helix131-1399
β-strand145-14845
β-strand155-16066
β-strand164-16966
α-helix170-1723
β-strand177-17935
α-helix1841
β-strand18515
α-helix1861
α-helix187-19711
β-strand202-20656
α-helix207-2126
α-helix213-22311
β-strand229-23356
α-helix234-2363
β-strand23717
β-strand24317
β-strand25212
α-helix253-2586
α-helix263-2719
β-strand27518
α-helix286-2927
α-helix295-2973
β-strand29818
β-strand30417
α-helix307-31610
α-helix317-3215
α-helix324-33714
α-helix345-35511
α-helix356-3583
α-helix364-3685
α-helix370-3723
α-helix381-40323
α-helix409-42214
α-helix427-43913
α-helix447-46721
Chain B: 33 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand3-649
α-helix141
β-strand15110
α-helix16-3116
β-strand35-3849
β-strand40111
α-helix52-6312
β-strand6919
β-strand70112
β-strand74112
β-strand81111
α-helix82-843
α-helix86-9813
β-strand102-105413
α-helix109-11911
α-helix125-1284
α-helix131-1399
β-strand145-148413
β-strand155-160614
β-strand164-169614
α-helix170-1723
β-strand177-179313
α-helix1841
β-strand185113
α-helix1861
α-helix187-19711
β-strand202-206514
α-helix207-2126
α-helix213-22311
α-helix225-2273
β-strand229-233514
α-helix234-2363
β-strand237115
β-strand243115
β-strand252110
α-helix253-2586
α-helix263-27210
α-helix286-2927
α-helix295-2973
α-helix3031
β-strand304115
α-helix3051
α-helix307-32014
α-helix324-33714
α-helix345-35511
α-helix356-3583
α-helix364-3685
α-helix370-3723
α-helix381-40222
α-helix409-42214
α-helix427-43913
α-helix447-4537
α-helix456-46712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
tRNAC, DRNA75
glutamyl-tRNA synthetaseA, Bprotein468Thermus thermophilusP27000 (AlphaFold model)
Sequence of entity 1 (C, D), FASTA
>2CV0_1 tRNA (chains C, D)
GGCCCCAUCGUCUAGCGGUUAGGACGCGGCCCUCUCAAGGCCGAAACGGGGGUUCGAUUC
CCCCUGGGGUCACCA
Sequence of entity 2 (A, B), FASTA
>2CV0_2 glutamyl-tRNA synthetase (chains A, B)
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL
KWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG
GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK
SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD
KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD
TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA
AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA

Ligands and cofactors

IDNameFormulaCopies
GLUGlutamic acidC5 H9 N O42
MGMagnesium ionMg2

Primary citation

Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase. Sekine, S., Shichiri, M., Bernier, S. et al. Structure (2006) 14:1791-1799. DOI 10.1016/j.str.2006.10.005 · PubMed

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

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