1NYL: Unliganded glutaminyl-tRNA synthetase

Unliganded glutaminyl-tRNA synthetase. Determined by X-ray diffraction at 2.6 Å resolution. Released 25 Feb 2003.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Escherichia coli
Chains
1
Atoms
4,240
Mol. weight
61.92 kDa
Released
25 Feb 2003

Explore 1NYL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 18 helices, 36 β-strands

ElementResiduesLengthSheet
α-helix10-2011
β-strand28-3141
β-strand4012
α-helix41-5616
β-strand60-6341
β-strand64-6523
α-helix77-8812
β-strand97-9823
α-helix99-1024
α-helix103-11513
β-strand119-12244
α-helix126-1327
α-helix150-16213
β-strand171-17444
α-helix183-1853
β-strand189-19354
β-strand207-20934
α-helix211-22212
β-strand226-23055
α-helix231-2333
α-helix236-24611
β-strand254-25855
α-helix259-2613
β-strand26316
α-helix270-2778
β-strand29212
α-helix293-2997
α-helix303-3108
β-strand32216
α-helix324-33815
β-strand341-34227
β-strand344-34527
β-strand348-35368
β-strand360-36459
β-strand378-38259
β-strand384-38858
α-helix389-3913
β-strand392110
β-strand403110
β-strand410111
β-strand411112
β-strand416111
β-strand419-42358
β-strand432-43548
β-strand456112
β-strand459-46028
β-strand465-47177
β-strand476113
β-strand491113
β-strand497-50377
α-helix505-5084
β-strand515-51847
β-strand522-52657
β-strand537-54267

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutaminyl-tRNA synthetaseAprotein539Escherichia coliP00962 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1NYL_1 Glutaminyl-tRNA synthetase (chains A)
TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDD
TNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPE
QIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRD
PVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNI
TIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIR
EFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEMVTMPN
HPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAE
GNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDF
LSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRD

Primary citation

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:

Browse structure collections

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