Crystal structure of Arginyl-tRNA synthetase. Determined by X-ray diffraction at 2.8 Å resolution. Released 23 Jul 2014.
Explore 4Q2Y in 3D Show helices and sheets RCSB PDB PDBe
4Q2Y contains 58 α-helices and 43 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 | 4-13 | 10 | |
| β-strand | 30-32 | 3 | 1 |
| β-strand | 41-43 | 3 | 1 |
| β-strand | 90-92 | 3 | 1 |
| α-helix | 93-95 | 3 | |
| α-helix | 96-109 | 14 | |
| β-strand | 121-125 | 5 | 2 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 134-135 | 2 | |
| α-helix | 137-155 | 19 | |
| β-strand | 159-164 | 6 | 2 |
| β-strand | 167 | 1 | 3 |
| α-helix | 172-183 | 12 | |
| α-helix | 197-210 | 14 | |
| α-helix | 212-226 | 15 | |
| α-helix | 230-253 | 24 | |
| β-strand | 259-260 | 2 | 2 |
| α-helix | 263-266 | 4 | |
| α-helix | 267-279 | 13 | |
| β-strand | 283-286 | 4 | 4 |
| β-strand | 289-292 | 4 | 4 |
| β-strand | 301-304 | 4 | 4 |
| β-strand | 310 | 1 | 4 |
| α-helix | 312-321 | 10 | |
| α-helix | 322-326 | 5 | |
| β-strand | 331-334 | 4 | 2 |
| β-strand | 337 | 1 | 5 |
| α-helix | 338-340 | 3 | |
| α-helix | 341-353 | 13 | |
| β-strand | 363-366 | 4 | 2 |
| β-strand | 369 | 1 | 5 |
| α-helix | 370-371 | 2 | |
| β-strand | 372-373 | 2 | 6 |
| β-strand | 379 | 1 | 6 |
| α-helix | 390-405 | 16 | |
| α-helix | 415-416 | 2 | |
| α-helix | 417-422 | 6 | |
| α-helix | 423-436 | 14 | |
| β-strand | 444-445 | 2 | 6 |
| α-helix | 448-452 | 5 | |
| α-helix | 459-469 | 11 | |
| α-helix | 473-476 | 4 | |
| α-helix | 480-489 | 10 | |
| α-helix | 497-506 | 10 | |
| α-helix | 509-519 | 11 | |
| α-helix | 523-540 | 18 | |
| β-strand | 547-548 | 2 | 7 |
| β-strand | 555-557 | 3 | 7 |
| α-helix | 560-579 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-17 | 14 | |
| β-strand | 30-32 | 3 | 8 |
| α-helix | 36-38 | 3 | |
| β-strand | 41-43 | 3 | 8 |
| α-helix | 45-48 | 4 | |
| α-helix | 67-72 | 6 | |
| β-strand | 79-82 | 4 | 8 |
| β-strand | 90-94 | 5 | 8 |
| α-helix | 95 | 1 | |
| α-helix | 96-109 | 14 | |
| β-strand | 121-125 | 5 | 9 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 10 |
| α-helix | 134-135 | 2 | |
| α-helix | 137-155 | 19 | |
| β-strand | 159-164 | 6 | 9 |
| β-strand | 167 | 1 | 10 |
| α-helix | 172-183 | 12 | |
| α-helix | 197-209 | 13 | |
| α-helix | 212-226 | 15 | |
| α-helix | 230-253 | 24 | |
| β-strand | 259-260 | 2 | 9 |
| α-helix | 263-266 | 4 | |
| α-helix | 267-279 | 13 | |
| β-strand | 283-286 | 4 | 11 |
| β-strand | 289-292 | 4 | 11 |
| β-strand | 301-304 | 4 | 11 |
| β-strand | 310 | 1 | 11 |
| α-helix | 312-325 | 14 | |
| β-strand | 331-334 | 4 | 9 |
| β-strand | 337 | 1 | 12 |
| α-helix | 338-340 | 3 | |
| α-helix | 341-353 | 13 | |
| β-strand | 363-366 | 4 | 9 |
| β-strand | 369 | 1 | 12 |
| α-helix | 370-371 | 2 | |
| β-strand | 372-373 | 2 | 13 |
| β-strand | 379 | 1 | 13 |
| α-helix | 390-405 | 16 | |
| α-helix | 415-419 | 5 | |
| α-helix | 421-436 | 16 | |
| β-strand | 444-445 | 2 | 13 |
| α-helix | 448-452 | 5 | |
| α-helix | 459-474 | 16 | |
| α-helix | 480-489 | 10 | |
| α-helix | 497-506 | 10 | |
| α-helix | 509-519 | 11 | |
| α-helix | 523-540 | 18 | |
| β-strand | 546-548 | 3 | 14 |
| β-strand | 555-558 | 4 | 14 |
| α-helix | 560-579 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Arginine--tRNA ligase, cytoplasmic | A, B | protein | 607 | Homo sapiens | P54136 (AlphaFold model) |
>4Q2Y_1 Arginine--tRNA ligase, cytoplasmic (chains A, B) HHHHHHSSGLVPRGSHMASMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDY QCNSAMGISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSE QLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVL RLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQC VVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRG FVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQS VHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRS MDKLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSRNRLNDYIFSFDKMLDDRGNTAAY LLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLF LHTLCDYIYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILG IKPVQRM
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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