Unliganded glutaminyl-tRNA synthetase. Determined by X-ray diffraction at 2.6 Å resolution. Released 25 Feb 2003.
Explore 1NYL in 3D Show helices and sheets RCSB PDB PDBe
1NYL contains 18 α-helices and 36 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 | 10-20 | 11 | |
| 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 | 77-88 | 12 | |
| β-strand | 97-98 | 2 | 3 |
| α-helix | 99-102 | 4 | |
| α-helix | 103-115 | 13 | |
| β-strand | 119-122 | 4 | 4 |
| α-helix | 126-132 | 7 | |
| α-helix | 150-162 | 13 | |
| β-strand | 171-174 | 4 | 4 |
| α-helix | 183-185 | 3 | |
| β-strand | 189-193 | 5 | 4 |
| β-strand | 207-209 | 3 | 4 |
| α-helix | 211-222 | 12 | |
| β-strand | 226-230 | 5 | 5 |
| α-helix | 231-233 | 3 | |
| α-helix | 236-246 | 11 | |
| β-strand | 254-258 | 5 | 5 |
| α-helix | 259-261 | 3 | |
| β-strand | 263 | 1 | 6 |
| α-helix | 270-277 | 8 | |
| β-strand | 292 | 1 | 2 |
| α-helix | 293-299 | 7 | |
| α-helix | 303-310 | 8 | |
| β-strand | 322 | 1 | 6 |
| α-helix | 324-338 | 15 | |
| β-strand | 341-342 | 2 | 7 |
| β-strand | 344-345 | 2 | 7 |
| β-strand | 348-353 | 6 | 8 |
| β-strand | 360-364 | 5 | 9 |
| β-strand | 378-382 | 5 | 9 |
| β-strand | 384-388 | 5 | 8 |
| α-helix | 389-391 | 3 | |
| β-strand | 392 | 1 | 10 |
| β-strand | 403 | 1 | 10 |
| β-strand | 410 | 1 | 11 |
| β-strand | 411 | 1 | 12 |
| β-strand | 416 | 1 | 11 |
| β-strand | 419-423 | 5 | 8 |
| β-strand | 432-435 | 4 | 8 |
| β-strand | 456 | 1 | 12 |
| β-strand | 459-460 | 2 | 8 |
| β-strand | 465-471 | 7 | 7 |
| β-strand | 476 | 1 | 13 |
| β-strand | 491 | 1 | 13 |
| β-strand | 497-503 | 7 | 7 |
| α-helix | 505-508 | 4 | |
| β-strand | 515-518 | 4 | 7 |
| β-strand | 522-526 | 5 | 7 |
| β-strand | 537-542 | 6 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutaminyl-tRNA synthetase | A | protein | 539 | Escherichia coli | P00962 (AlphaFold model) |
>1NYL_1 Glutaminyl-tRNA synthetase (chains A) TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDD TNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPE QIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRD PVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI TIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIR EFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEMVTMPN HPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAE GNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDF LSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRD
tRNA-Dependent Active Site Assembly in a Class I Aminoacyl-tRNA Synthetase. Sherlin, L.D., Perona, J.J. Structure (2003) 11:591-603. DOI 10.1016/S0969-2126(03)00074-1 · 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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