Crystal structure of glutaminyl-tRNA synthetase complexed with a tRNA-gln mutant and an active-site inhibitor. Determined by X-ray diffraction at 3.1 Å resolution. Released 4 Jun 2000.
Explore 1EUQ in 3D Show helices and sheets RCSB PDB PDBe
1EUQ contains 23 α-helices and 44 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 |
|---|---|---|---|
| α-helix | 10-21 | 12 | |
| β-strand | 28-31 | 4 | 1 |
| β-strand | 40 | 1 | 2 |
| α-helix | 41-56 | 16 | |
| β-strand | 60-63 | 4 | 1 |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 70-72 | 3 | |
| α-helix | 75-88 | 14 | |
| β-strand | 97-98 | 2 | 3 |
| α-helix | 99-102 | 4 | |
| α-helix | 103-115 | 13 | |
| β-strand | 119-122 | 4 | 4 |
| α-helix | 126-133 | 8 | |
| α-helix | 150-161 | 12 | |
| β-strand | 171-174 | 4 | 4 |
| α-helix | 183-185 | 3 | |
| β-strand | 189-193 | 5 | 4 |
| β-strand | 198 | 1 | 5 |
| β-strand | 202 | 1 | 5 |
| β-strand | 207-209 | 3 | 4 |
| α-helix | 211-222 | 12 | |
| β-strand | 226-230 | 5 | 6 |
| α-helix | 231-234 | 4 | |
| α-helix | 237-244 | 8 | |
| β-strand | 254-258 | 5 | 6 |
| α-helix | 259-261 | 3 | |
| β-strand | 263 | 1 | 7 |
| β-strand | 266 | 1 | 7 |
| α-helix | 272-278 | 7 | |
| β-strand | 292 | 1 | 2 |
| α-helix | 293-299 | 7 | |
| α-helix | 303-312 | 10 | |
| β-strand | 322 | 1 | 7 |
| α-helix | 324-338 | 15 | |
| α-helix | 339-340 | 2 | |
| β-strand | 341-342 | 2 | 8 |
| β-strand | 344-345 | 2 | 8 |
| β-strand | 348-352 | 5 | 9 |
| β-strand | 353 | 1 | 10 |
| β-strand | 363-366 | 4 | 11 |
| α-helix | 372-374 | 3 | |
| β-strand | 376-379 | 4 | 11 |
| β-strand | 384-388 | 5 | 9 |
| α-helix | 389-391 | 3 | |
| β-strand | 392-393 | 2 | 12 |
| β-strand | 403-404 | 2 | 12 |
| β-strand | 410-411 | 2 | 13 |
| β-strand | 416 | 1 | 13 |
| β-strand | 419 | 1 | 10 |
| β-strand | 424 | 1 | 14 |
| β-strand | 430 | 1 | 14 |
| β-strand | 432 | 1 | 9 |
| β-strand | 435 | 1 | 10 |
| β-strand | 455-456 | 2 | 13 |
| β-strand | 459-460 | 2 | 9 |
| β-strand | 465-472 | 8 | 8 |
| β-strand | 476 | 1 | 15 |
| α-helix | 481-483 | 3 | |
| α-helix | 487-490 | 4 | |
| β-strand | 491 | 1 | 15 |
| β-strand | 496-503 | 8 | 8 |
| α-helix | 506-509 | 4 | |
| β-strand | 512 | 1 | 16 |
| β-strand | 514 | 1 | 16 |
| β-strand | 515-518 | 4 | 8 |
| β-strand | 522-526 | 5 | 8 |
| β-strand | 537-543 | 7 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutaminyl tRNA | B | RNA | 72 | ||
| Glutaminyl-tRNA synthetase | A | protein | 548 | Escherichia coli | P00962 (AlphaFold model) |
>1EUQ_1 GLUTAMINYL TRNA (chains B) GGGGUAUCGCCAAGCGGUAAGGCACCGGAUUCUGAUUCCGGCAGCGAGGUUCGAAUCCUC GUACCCCAGCCA
>1EUQ_2 GLUTAMINYL-TRNA SYNTHETASE (chains A) MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKG QCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLA YVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMA SPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL YDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRR GYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGE GEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKA ERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVP NPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFN RTVGLRDT
| ID | Name | Formula | Copies |
|---|---|---|---|
| QSI | 5'-O-[N-(L-glutaminyl)-sulfamoyl]adenosine | C15 H22 N8 O8 S | 1 |
Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases. Sherlin, L.D., Bullock, T.L., Newberry, K.J. et al. J Mol Biol (2000) 299:431-446. DOI 10.1006/jmbi.2000.3749 · PubMed
Other PDB entries of the same protein (UniProt P00962 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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