Crystal Structure of human lysyl-tRNA synthetase with acetyllysine. Determined by X-ray diffraction at 2.26 Å resolution. Released 22 Jan 2025.
Explore 8XP4 in 3D Show helices and sheets RCSB PDB PDBe
8XP4 contains 55 α-helices and 46 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 | 73-89 | 17 | |
| 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 | 166-175 | 10 | |
| β-strand | 181-190 | 10 | 1 |
| β-strand | 196-207 | 12 | 1 |
| α-helix | 212-215 | 4 | |
| α-helix | 223-228 | 6 | |
| α-helix | 230-236 | 7 | |
| α-helix | 238-259 | 22 | |
| α-helix | 263 | 1 | |
| 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 | 349-366 | 18 | |
| β-strand | 370-373 | 4 | 5 |
| β-strand | 383-386 | 4 | 5 |
| α-helix | 388 | 1 | |
| α-helix | 391 | 1 | |
| β-strand | 392-395 | 4 | 2 |
| α-helix | 396-404 | 9 | |
| α-helix | 407-410 | 4 | |
| α-helix | 411-413 | 3 | |
| α-helix | 417-429 | 13 | |
| α-helix | 440-451 | 12 | |
| α-helix | 453-455 | 3 | |
| β-strand | 460-463 | 4 | 2 |
| β-strand | 466 | 1 | 6 |
| β-strand | 482 | 1 | 6 |
| β-strand | 485-490 | 6 | 2 |
| β-strand | 493-500 | 8 | 2 |
| α-helix | 501-502 | 2 | |
| α-helix | 505-517 | 13 | |
| α-helix | 531-540 | 10 | |
| α-helix | 541-542 | 2 | |
| 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 | 105-112 | 8 | |
| α-helix | 115-116 | 2 | |
| β-strand | 120 | 1 | 7 |
| β-strand | 126-137 | 12 | 7 |
| β-strand | 142-149 | 8 | 7 |
| β-strand | 152-159 | 8 | 7 |
| α-helix | 166-173 | 8 | |
| β-strand | 181-190 | 10 | 7 |
| β-strand | 196-207 | 12 | 7 |
| α-helix | 212-215 | 4 | |
| α-helix | 223-228 | 6 | |
| α-helix | 230-236 | 7 | |
| α-helix | 238-260 | 23 | |
| β-strand | 264-265 | 2 | 8 |
| 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 | 301-309 | 9 | |
| β-strand | 314-322 | 9 | 8 |
| β-strand | 328 | 1 | 9 |
| β-strand | 331 | 1 | 9 |
| β-strand | 334-343 | 10 | 8 |
| α-helix | 349-366 | 18 | |
| β-strand | 370-373 | 4 | 10 |
| α-helix | 381-382 | 2 | |
| β-strand | 383-386 | 4 | 10 |
| α-helix | 388 | 1 | |
| α-helix | 391 | 1 | |
| β-strand | 392-395 | 4 | 8 |
| α-helix | 396-404 | 9 | |
| α-helix | 407-410 | 4 | |
| α-helix | 411-413 | 3 | |
| α-helix | 417-429 | 13 | |
| α-helix | 435 | 1 | |
| α-helix | 437 | 1 | |
| α-helix | 440-451 | 12 | |
| α-helix | 453-455 | 3 | |
| β-strand | 460-463 | 4 | 8 |
| β-strand | 466 | 1 | 11 |
| β-strand | 482 | 1 | 11 |
| β-strand | 485-490 | 6 | 8 |
| β-strand | 493-500 | 8 | 8 |
| α-helix | 501-502 | 2 | |
| α-helix | 505-511 | 7 | |
| α-helix | 531-538 | 8 | |
| α-helix | 541-542 | 2 | |
| β-strand | 544-550 | 7 | 8 |
| α-helix | 551-558 | 8 | |
| α-helix | 564-566 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine--tRNA ligase | A, B | protein | 520 | Homo sapiens | Q15046 (AlphaFold model) |
>8XP4_1 Lysine--tRNA ligase (chains A, B) MSVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKV AGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNP GKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRS KIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLV VGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGS YKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETRKILDDICV AKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFEL FVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWG MGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKELEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ALY | N(6)-acetyllysine | C8 H16 N2 O3 | 2 |
Co-Translational Deposition of N6-Acetyl-L-Lysine in Nascent Proteins Contributes to the Acetylome in Mammalian Cells. Guo, D., Li, N., Zhang, X. et al. Adv Sci (Weinh) (2025) 12:2403309. DOI 10.1002/advs.202403309
Other PDB entries of the same protein (UniProt Q15046 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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