Human LysRS bound to unmodified tRNA-Lys3 (Undocked State, AMPCPP bound). Determined by electron microscopy at 2.9 Å resolution. Released 12 Mar 2025.
Explore 9DPB in 3D Show helices and sheets RCSB PDB PDBe
9DPB contains 43 α-helices and 51 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 76-89 | 14 | |
| α-helix | 105-112 | 8 | |
| 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 | 166-173 | 8 | |
| β-strand | 181-190 | 10 | 1 |
| β-strand | 196-207 | 12 | 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 | 281-283 | 3 | |
| 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 | 347-366 | 20 | |
| β-strand | 370-373 | 4 | 5 |
| β-strand | 383-386 | 4 | 5 |
| β-strand | 392-394 | 3 | 2 |
| α-helix | 396-404 | 9 | |
| α-helix | 407-410 | 4 | |
| α-helix | 411-414 | 4 | |
| 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 | 6 |
| β-strand | 473 | 1 | 7 |
| α-helix | 474 | 1 | |
| β-strand | 475 | 1 | 6 |
| α-helix | 476 | 1 | |
| β-strand | 482-483 | 2 | 6 |
| β-strand | 485-490 | 6 | 2 |
| β-strand | 493-500 | 8 | 2 |
| β-strand | 501 | 1 | 7 |
| α-helix | 505-520 | 16 | |
| α-helix | 531-537 | 7 | |
| β-strand | 544-550 | 7 | 2 |
| α-helix | 551-558 | 8 | |
| α-helix | 564-566 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 73-89 | 17 | |
| α-helix | 105-111 | 7 | |
| α-helix | 115-116 | 2 | |
| β-strand | 120 | 1 | 8 |
| β-strand | 126-137 | 12 | 8 |
| β-strand | 142-148 | 7 | 8 |
| β-strand | 153 | 1 | 8 |
| β-strand | 156-159 | 4 | 8 |
| α-helix | 166-173 | 8 | |
| β-strand | 181-190 | 10 | 8 |
| β-strand | 196-207 | 12 | 8 |
| α-helix | 212-213 | 2 | |
| α-helix | 223-228 | 6 | |
| α-helix | 230-236 | 7 | |
| α-helix | 239-260 | 22 | |
| β-strand | 264-265 | 2 | 9 |
| β-strand | 271-272 | 2 | 10 |
| β-strand | 284 | 1 | 10 |
| α-helix | 292-294 | 3 | |
| β-strand | 295-296 | 2 | 10 |
| α-helix | 301-310 | 10 | |
| β-strand | 314-322 | 9 | 9 |
| β-strand | 334-343 | 10 | 9 |
| α-helix | 349-366 | 18 | |
| β-strand | 370-373 | 4 | 11 |
| β-strand | 383-386 | 4 | 11 |
| β-strand | 392-394 | 3 | 9 |
| α-helix | 398-404 | 7 | |
| α-helix | 417-429 | 13 | |
| α-helix | 440-451 | 12 | |
| β-strand | 460-462 | 3 | 9 |
| β-strand | 464-466 | 3 | 12 |
| α-helix | 467-469 | 3 | |
| β-strand | 473 | 1 | 13 |
| α-helix | 474 | 1 | |
| β-strand | 475 | 1 | 12 |
| α-helix | 476 | 1 | |
| β-strand | 482-484 | 3 | 12 |
| β-strand | 485-490 | 6 | 9 |
| β-strand | 493-500 | 8 | 9 |
| β-strand | 501 | 1 | 13 |
| α-helix | 505-521 | 17 | |
| α-helix | 531-538 | 8 | |
| β-strand | 544-550 | 7 | 9 |
| α-helix | 551-558 | 8 |
| 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 |
>9DPB_1 Lysine--tRNA ligase (chains A, B) MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTT DNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH LTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGD IIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAP ELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSG MVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETR KILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYG LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
>9DPB_2 tRNA-Lys3 (unmodified) (chains C) GCCCGGAUAGCUCAGUCGGUAGAGCAUCAGACUUUUAAUCUGAGGGUCCAGGGUUCAAGU CCCUGUUCGGGCGCCA
| ID | Name | Formula | Copies |
|---|---|---|---|
| LYS | Lysine | C6 H15 N2 O2 | 2 |
| APC | Diphosphomethylphosphonic acid adenosyl ester | C11 H18 N5 O12 P3 | 2 |
| MG | Magnesium ion | Mg | 4 |
Water and common crystallization additives (NA) are not listed.
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:
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