4JXZ: E. coli glutaminyl-tRNA synthetase

Structure of E. coli glutaminyl-tRNA synthetase bound to ATP and a tRNA(Gln) acceptor containing a UUG anticodon. Determined by X-ray diffraction at 2.4 Å resolution. Released 1 May 2013.

Method
X-ray diffraction
Resolution
2.4 Å
Organisms
Escherichia coli, synthetic construct
Chains
2
Atoms
6,027
Mol. weight
88.2 kDa
Ligands
ATP
Released
1 May 2013

Explore 4JXZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JXZ contains 24 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: 24 helices, 36 β-strands

ElementResiduesLengthSheet
α-helix10-2112
β-strand28-3141
β-strand4012
α-helix41-5616
β-strand60-6341
β-strand64-6523
α-helix70-723
α-helix75-8713
β-strand97-9823
α-helix99-1024
α-helix103-11513
β-strand119-12244
α-helix126-1338
α-helix150-16213
β-strand171-17444
α-helix183-1853
β-strand189-19354
β-strand19815
β-strand20215
β-strand207-20934
α-helix211-22212
β-strand226-23056
α-helix231-2333
α-helix237-2459
β-strand254-25856
α-helix259-2613
β-strand26317
α-helix270-2789
β-strand29212
α-helix293-2997
α-helix303-31311
β-strand32217
α-helix324-33815
α-helix339-3402
β-strand341-34228
β-strand344-34528
β-strand348-35369
β-strand361-366610
α-helix372-3743
β-strand376-381610
β-strand384-38859
α-helix389-3913
β-strand392-393211
β-strand403-404211
β-strand410-41129
β-strand416-42499
β-strand430-43899
β-strand455-45629
β-strand459-46029
β-strand465-47288
β-strand476112
α-helix481-4833
α-helix487-4904
β-strand491112
β-strand496-50388
α-helix505-5095
β-strand515-51848
β-strand522-52658
β-strand537-54268
α-helix543-5453

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamine--tRNA ligaseAprotein553Escherichia coliP00962 (AlphaFold model)
RNA (71-mer)BRNA75synthetic construct
Sequence of entity 1 (A), FASTA
>4JXZ_1 Glutamine--tRNA ligase (chains A)
SEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQ
CNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAY
VDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMAS
PFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLY
DWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRG
YTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEG
EMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAE
RVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPN
PGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNR
TVGLRDTWAKVGE
Sequence of entity 2 (B), FASTA
>4JXZ_2 RNA (71-MER) (chains B)
UGGGGUAUCGCCAAGCGGUAAGGCACCGGUUUUUGAUACCGGCAUUCGCAGGUUCGAAUC
CUGCUACCCCAGCCA

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structural and Mechanistic Basis for Enhanced Translational Efficiency by 2-Thiouridine at the tRNA Anticodon Wobble Position. Rodriguez-Hernandez, A., Spears, J.L., Gaston, K.W. et al. J Mol Biol (2013) 425:3888-3906. DOI 10.1016/j.jmb.2013.05.018 · 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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