Glutamyl-tRNA synthetase from Thermus thermophilus in complex with L-glutamate. Determined by X-ray diffraction at 1.98 Å resolution. Released 5 Sept 2006.
Explore 2CUZ in 3D Show helices and sheets RCSB PDB PDBe
2CUZ contains 32 α-helices and 20 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 1 |
| α-helix | 14 | 1 | |
| β-strand | 15 | 1 | 2 |
| α-helix | 16-31 | 16 | |
| β-strand | 35-38 | 4 | 1 |
| β-strand | 40 | 1 | 3 |
| α-helix | 52-62 | 11 | |
| β-strand | 69 | 1 | 1 |
| β-strand | 70 | 1 | 4 |
| β-strand | 74 | 1 | 4 |
| β-strand | 81 | 1 | 3 |
| α-helix | 82-84 | 3 | |
| α-helix | 86-99 | 14 | |
| β-strand | 102-105 | 4 | 5 |
| α-helix | 109-119 | 11 | |
| α-helix | 125-128 | 4 | |
| α-helix | 131-139 | 9 | |
| β-strand | 145-148 | 4 | 5 |
| β-strand | 155-160 | 6 | 6 |
| β-strand | 164-169 | 6 | 6 |
| α-helix | 170-172 | 3 | |
| β-strand | 177-179 | 3 | 5 |
| α-helix | 184 | 1 | |
| β-strand | 185 | 1 | 5 |
| α-helix | 186 | 1 | |
| α-helix | 187-197 | 11 | |
| β-strand | 202-206 | 5 | 6 |
| α-helix | 207-212 | 6 | |
| α-helix | 213-223 | 11 | |
| β-strand | 229-233 | 5 | 6 |
| α-helix | 234-236 | 3 | |
| β-strand | 237 | 1 | 7 |
| β-strand | 243 | 1 | 7 |
| β-strand | 252 | 1 | 2 |
| α-helix | 253-258 | 6 | |
| α-helix | 263-271 | 9 | |
| α-helix | 286-292 | 7 | |
| α-helix | 295-297 | 3 | |
| β-strand | 304 | 1 | 7 |
| α-helix | 307-316 | 10 | |
| α-helix | 317-321 | 5 | |
| α-helix | 324-337 | 14 | |
| α-helix | 345-355 | 11 | |
| α-helix | 356-358 | 3 | |
| α-helix | 364-368 | 5 | |
| α-helix | 370-372 | 3 | |
| α-helix | 381-403 | 23 | |
| α-helix | 409-422 | 14 | |
| α-helix | 427-439 | 13 | |
| α-helix | 447-454 | 8 | |
| α-helix | 456-463 | 8 | |
| α-helix | 464-466 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamyl-tRNA synthetase | A | protein | 468 | Thermus thermophilus | P27000 (AlphaFold model) |
>2CUZ_1 Glutamyl-tRNA synthetase (chains A) MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL KWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA
| ID | Name | Formula | Copies |
|---|---|---|---|
| GLU | Glutamic acid | C5 H9 N O4 | 1 |
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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