4YE9: G45V mutant of human GlnRS

The crystal structure of the G45V mutant of human GlnRS. Determined by X-ray diffraction at 2.7 Å resolution. Released 17 Feb 2016.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Homo sapiens
Chains
1
Atoms
5,288
Mol. weight
88.1 kDa
Released
17 Feb 2016

Explore 4YE9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4YE9 contains 31 α-helices and 34 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: 31 helices, 34 β-strands

ElementResiduesLengthSheet
α-helix6-116
α-helix17-259
α-helix27-4418
α-helix47-493
α-helix50-6011
α-helix69-779
α-helix84-9613
α-helix104-1096
α-helix119-13113
α-helix134-1407
α-helix141-1433
α-helix147-15610
α-helix162-17716
α-helix220-2234
α-helix226-2283
α-helix231-2333
α-helix237-2393
α-helix249-26012
β-strand265-26841
β-strand27712
α-helix280-29314
β-strand297-30261
α-helix312-32413
β-strand331-33441
α-helix335-3384
α-helix339-35113
β-strand355-35843
α-helix371-3733
α-helix380-39112
β-strand401-40443
β-strand40714
β-strand41314
β-strand416-42053
α-helix4241
β-strand42515
β-strand42915
β-strand434-43633
α-helix438-44811
β-strand453-45756
α-helix464-47310
β-strand480-48456
β-strand488-48927
α-helix496-5027
β-strand51812
α-helix519-5257
α-helix529-5368
β-strand547-54827
α-helix551-56414
β-strand567-56828
β-strand570-57128
β-strand575-57629
β-strand577-578210
β-strand590-593411
β-strand603-606411
β-strand613-61429
β-strand649-650210
β-strand661-662210
β-strand68119
β-strand685-69288
β-strand696112
β-strand715112
β-strand720-72898
β-strand740-74348
β-strand747-75158
β-strand761-76668

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamine--tRNA ligaseAprotein776Homo sapiensP47897 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4YE9_1 Glutamine--tRNA ligase (chains A)
HMAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLVSTIDKATGILLYGL
ASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTP
EQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGP
KLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYK
TPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICF
LRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCH
QRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYR
VKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCP
VQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARV
GVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADE
TKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVE
SLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLAS
LHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV

Primary citation

The crystal structure of human GlnRS provides basis for the development of neurological disorders. Ognjenovic, J., Wu, J., Matthies, D. et al. Nucleic Acids Res (2016) 44:3420-3431. DOI 10.1093/nar/gkw082 · PubMed

Other PDB entries of the same protein (UniProt P47897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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