4Q2T: Arginyl-tRNA synthetase

Crystal structure of Arginyl-tRNA synthetase complexed with L-arginine. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Jul 2014.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
2
Atoms
9,765
Mol. weight
139.23 kDa
Ligands
ARG
Released
23 Jul 2014

Explore 4Q2T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Q2T contains 64 α-helices and 40 β-strands across 2 chains. 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: 32 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix4-1916
β-strand30-3231
α-helix36-383
β-strand41-4331
α-helix45-539
α-helix62-709
α-helix73-753
β-strand79-8571
β-strand89-9461
α-helix96-10813
α-helix113-1164
β-strand121-12552
α-helix1291
β-strand13013
α-helix134-1352
α-helix137-15519
β-strand159-16462
β-strand16713
α-helix174-18310
α-helix197-21014
α-helix212-22615
α-helix230-25324
β-strand259-26022
α-helix263-2664
α-helix267-27913
β-strand284-28634
β-strand289-29244
α-helix293-2942
β-strand301-30444
α-helix312-32514
β-strand331-33772
α-helix338-3403
α-helix341-35313
β-strand363-36972
β-strand372-37325
β-strand37915
β-strand38216
β-strand38616
α-helix387-3893
α-helix390-40516
α-helix409-4113
α-helix417-4226
α-helix423-43614
β-strand444-44525
α-helix448-4525
α-helix459-47416
α-helix480-48910
α-helix497-50610
α-helix509-51911
α-helix523-54018
β-strand54617
β-strand55817
α-helix560-57920
Chain B: 32 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix4-1916
β-strand30-3238
α-helix36-383
β-strand41-4338
α-helix45-539
α-helix62-709
α-helix73-753
β-strand79-8578
β-strand89-9468
α-helix96-10914
α-helix113-1164
β-strand121-12559
α-helix1291
β-strand130110
α-helix134-1352
α-helix137-15519
β-strand159-16469
β-strand167110
α-helix172-18312
α-helix197-21014
α-helix212-22615
α-helix230-25324
β-strand259-26029
α-helix263-2664
α-helix267-27913
β-strand284-286311
β-strand289-292411
α-helix293-2942
β-strand301-304411
α-helix312-32514
β-strand331-33559
α-helix338-3403
α-helix341-35313
β-strand363-36759
β-strand372-373212
β-strand379112
α-helix387-3893
α-helix390-40516
α-helix409-4113
α-helix417-4226
α-helix423-43614
β-strand444-445212
α-helix448-4525
α-helix459-47416
α-helix480-48910
α-helix497-50610
α-helix509-51911
α-helix523-54018
β-strand546-547213
β-strand557-558213
α-helix560-57920

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Arginine--tRNA ligase, cytoplasmicA, Bprotein607Homo sapiensP54136 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4Q2T_1 Arginine--tRNA ligase, cytoplasmic (chains A, B)
HHHHHHSSGLVPRGSHMASMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDY
QCNSAMGISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSE
QLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVL
RLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQC
VVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRG
FVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQS
VHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRS
MDKLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSRNRLNDYIFSFDKMLDDRGNTAAY
LLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLF
LHTLCDYIYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILG
IKPVQRM

Ligands and cofactors

IDNameFormulaCopies
ARGArginineC6 H15 N4 O22

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

Primary citation

The crystal structure of arginyl-tRNA synthetase from Homo sapiens. Kim, H.S., Cha, S.Y., Jo, C.H. et al. FEBS Lett (2014) 588:2328-2334. DOI 10.1016/j.febslet.2014.05.027 · PubMed

Other PDB entries of the same protein (UniProt P54136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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