Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP. Determined by X-ray diffraction at 1.9 Å resolution. Released 25 Feb 2003.
Explore 1N75 in 3D Show helices and sheets RCSB PDB PDBe
1N75 contains 35 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 | |
| α-helix | 225-227 | 3 | |
| β-strand | 229-233 | 5 | 6 |
| α-helix | 234-236 | 3 | |
| β-strand | 237 | 1 | 7 |
| α-helix | 242 | 1 | |
| β-strand | 243 | 1 | 7 |
| α-helix | 244 | 1 | |
| 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 | |
| α-helix | 302-303 | 2 | |
| 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 | 381-402 | 22 | |
| α-helix | 409-423 | 15 | |
| α-helix | 427-439 | 13 | |
| α-helix | 447-453 | 7 | |
| α-helix | 456-467 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamyl-tRNA synthetase | A | protein | 468 | Thermus thermophilus | P27000 (AlphaFold model) |
>1N75_1 Glutamyl-tRNA synthetase (chains A) MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVPGAEERILAAL KWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRGWAYRAFETPEELEQIRKEKG GYDGRARNIPPEEAEERARRGEPHVIRLKVPRPGTTEVKDELRGVVVYDNQEIPDVVLLK SDGYPTYHLANVVDDHLMGVTDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPD KTKISKRKSHTSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRRAVELMRPRFD TLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPRLRAQEEWTEAALEALLRGFA AEKGVKLGQVAQPLRAALTGSLETPGLFEILALLGKERALRRLERALA
ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. Sekine, S., Nureki, O., Dubois, D.Y. et al. EMBO J (2003) 22:676-688. DOI 10.1093/emboj/cdg053 · 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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