9DOW: H-LysRS

h-LysRS bound to unmodified tRNA-Lys3 (Undocked State, AMP bound). Determined by electron microscopy at 3.1 Å resolution. Released 12 Mar 2025.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 3
Atoms: 9,816
Mol. weight: 161.75 kDa
Ligands: LYS, AMP
Released: 12 Mar 2025

Explore 9DOW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9DOW contains 48 α-helices and 48 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: 25 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	75-89	15
α-helix	105-111	7
α-helix	112-114	3
α-helix	115-116	2
β-strand	120	1	1
β-strand	126-137	12	1
β-strand	142-149	8	1
β-strand	152-159	8	1
α-helix	160-162	3
α-helix	166-175	10
β-strand	181-190	10	1
β-strand	196-200	5	1
β-strand	204-207	4	1
α-helix	225-228	4
α-helix	230-236	7
α-helix	239-260	22
β-strand	264-265	2	2
β-strand	271-272	2	3
α-helix	281-282	2
β-strand	284-287	4	3
β-strand	292-296	5	3
α-helix	301-310	10
β-strand	314-322	9	2
β-strand	328	1	4
β-strand	331	1	4
β-strand	334-343	10	2
α-helix	347-365	19
β-strand	370-373	4	5
β-strand	375	1	6
β-strand	377	1	6
β-strand	383-386	4	5
β-strand	392-394	3	2
α-helix	396-404	9
α-helix	408-410	3
α-helix	411-413	3
α-helix	417-429	13
α-helix	440-451	12
α-helix	453-455	3
β-strand	460-462	3	2
β-strand	465-466	2	7
α-helix	474	1
β-strand	475	1	7
α-helix	476	1
β-strand	482-483	2	7
β-strand	486-490	5	2
β-strand	493-498	6	2
β-strand	500	1	2
α-helix	505-515	11
α-helix	516-520	5
α-helix	531-538	8
β-strand	544-550	7	2
α-helix	551-558	8
α-helix	564-566	3

Chain B: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	73-89	17
α-helix	105-112	8
β-strand	120	1	8
β-strand	126-138	13	8
β-strand	142-148	7	8
β-strand	153-158	6	8
α-helix	166-175	10
β-strand	181-190	10	8
β-strand	196-207	12	8
α-helix	212-214	3
α-helix	223-228	6
α-helix	230-236	7
α-helix	239-260	22
β-strand	265	1	9
β-strand	271-272	2	3
β-strand	284-287	4	3
β-strand	292-296	5	3
α-helix	297	1
α-helix	302-310	9
β-strand	314-322	9	9
β-strand	334-343	10	9
α-helix	347-365	19
β-strand	370-373	4	10
β-strand	383-386	4	10
β-strand	392-395	4	9
α-helix	396-404	9
α-helix	408-410	3
α-helix	419-429	11
α-helix	440-451	12
α-helix	453-455	3
β-strand	460-466	7	9
α-helix	467-469	3
α-helix	474	1
β-strand	475	1	9
α-helix	476	1
β-strand	482-490	9	9
β-strand	493-500	8	9
α-helix	505-520	16
α-helix	531-538	8
β-strand	544-550	7	9
α-helix	551-558	8
α-helix	564-567	4
α-helix	573-575	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lysine--tRNA ligase	A, B	protein	597	Homo sapiens	Q15046 (AlphaFold model)
tRNA-Lys3 (Unmodified)	C	RNA	76	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>9DOW_1 Lysine--tRNA ligase (chains A, B)
MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTT
DNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH
LTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGD
IIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAP
ELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSG
MVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETR
KILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYG
LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV

Sequence of entity 2 (C), FASTA

>9DOW_2 tRNA-Lys3 (Unmodified) (chains C)
GCCCGGAUAGCUCAGUCGGUAGAGCAUCAGACUUUUAAUCUGAGGGUCCAGGGUUCAAGU
CCCUGUUCGGGCGCCA

Ligands and cofactors

ID	Name	Formula	Copies
LYS	Lysine	C6 H15 N2 O2	2
AMP	Adenosine monophosphate	C10 H14 N5 O7 P	2

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

Primary citation

Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase. Devarkar, S.C., Budding, C.R., Pathirage, C. et al. Nucleic Acids Res (2025) 53. DOI 10.1093/nar/gkaf114 · PubMed

Other PDB entries of the same protein (UniProt Q15046 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ILD 1.88 Å, Crystal Structure of Human LysRS: P38/AIMP2 Complex II
4YCU 2.1 Å, Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase
8XP4 2.26 Å, Crystal Structure of human lysyl-tRNA synthetase with acetyllysine
3BJU 2.31 Å, Crystal Structure of tetrameric form of human lysyl-tRNA synthetase
6CHD 2.5 Å, Crystal Structure of Human Lysyl-tRNA Synthetase complexed with L-Lysylsulfamoyl Adenosine
7EA9 2.5 Å, Crystal Structure of human lysyl-tRNA synthetase Y145H mutant
6ILH 2.5 Å, Crystal Structure of human lysyl-tRNA synthetase L350H mutant
8HYR 2.55 Å, Crystal structure of human KARS apo
9DPL 2.8 Å, Human LysRS bound to cellular modified tRNA-Lys3 and AIMP2
4DPG 2.84 Å, Crystal Structure of Human LysRS: P38/AIMP2 Complex I
4YCW 2.9 Å, Crystal structure of cladosporin in complex with plasmodium like human lysyl-tRNA…
9DPB 2.9 Å, Human LysRS bound to unmodified tRNA-Lys3 (Undocked State, AMPCPP bound)

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