Insights into editing from an ile-tRNA synthetase structure with trna(ile) and mupirocin. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 Aug 1999.
Explore 1QU3 in 3D Show helices and sheets RCSB PDB PDBe
1QU3 contains 46 α-helices and 45 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-34 | 15 | |
| α-helix | 36-44 | 9 | |
| β-strand | 49 | 1 | 1 |
| α-helix | 53-55 | 3 | |
| β-strand | 58 | 1 | 2 |
| α-helix | 65-83 | 19 | |
| β-strand | 87 | 1 | 1 |
| β-strand | 93-94 | 2 | 3 |
| β-strand | 95 | 1 | 2 |
| α-helix | 100-106 | 7 | |
| α-helix | 118-121 | 4 | |
| α-helix | 122-124 | 3 | |
| α-helix | 126-141 | 16 | |
| β-strand | 152-153 | 2 | 3 |
| α-helix | 157-171 | 15 | |
| β-strand | 178-185 | 8 | 4 |
| β-strand | 192 | 1 | 4 |
| α-helix | 195-197 | 3 | |
| β-strand | 198-200 | 3 | 5 |
| β-strand | 208-209 | 2 | 6 |
| β-strand | 212 | 1 | 7 |
| β-strand | 213-214 | 2 | 8 |
| α-helix | 218-220 | 3 | |
| β-strand | 227 | 1 | 7 |
| β-strand | 230-231 | 2 | 6 |
| α-helix | 237-239 | 3 | |
| β-strand | 242-245 | 4 | 9 |
| β-strand | 262 | 1 | 7 |
| α-helix | 268-274 | 7 | |
| α-helix | 290-293 | 4 | |
| β-strand | 298-299 | 2 | 8 |
| α-helix | 301-303 | 3 | |
| β-strand | 307-308 | 2 | 8 |
| β-strand | 309-312 | 4 | 9 |
| β-strand | 326 | 1 | 9 |
| α-helix | 332-339 | 8 | |
| β-strand | 356 | 1 | 10 |
| β-strand | 358 | 1 | 10 |
| α-helix | 361-364 | 4 | |
| α-helix | 369-378 | 10 | |
| α-helix | 380-383 | 4 | |
| β-strand | 387 | 1 | 6 |
| β-strand | 395-397 | 3 | 5 |
| β-strand | 402-403 | 2 | 5 |
| β-strand | 405-412 | 8 | 4 |
| β-strand | 413-414 | 2 | 11 |
| α-helix | 416-419 | 4 | |
| α-helix | 422-428 | 7 | |
| β-strand | 431-432 | 2 | 12 |
| α-helix | 436-448 | 13 | |
| β-strand | 451-452 | 2 | 11 |
| β-strand | 455 | 1 | 13 |
| β-strand | 462 | 1 | 13 |
| β-strand | 466-467 | 2 | 14 |
| β-strand | 474 | 1 | 14 |
| α-helix | 479-490 | 12 | |
| α-helix | 494-497 | 4 | |
| α-helix | 501-503 | 3 | |
| β-strand | 519-520 | 2 | 14 |
| β-strand | 524 | 1 | 13 |
| α-helix | 528-532 | 5 | |
| α-helix | 534 | 1 | |
| α-helix | 535-539 | 5 | |
| β-strand | 549-555 | 7 | 12 |
| α-helix | 556-558 | 3 | |
| α-helix | 564-574 | 11 | |
| β-strand | 579-585 | 7 | 12 |
| β-strand | 588-589 | 2 | 15 |
| α-helix | 607-613 | 7 | |
| α-helix | 615-622 | 8 | |
| β-strand | 631-632 | 2 | 15 |
| α-helix | 635-657 | 23 | |
| α-helix | 671-673 | 3 | |
| α-helix | 676-697 | 22 | |
| α-helix | 702-710 | 9 | |
| α-helix | 711-721 | 11 | |
| α-helix | 722-728 | 7 | |
| α-helix | 736-748 | 13 | |
| α-helix | 750-756 | 7 | |
| α-helix | 761-769 | 9 | |
| α-helix | 779-781 | 3 | |
| α-helix | 783-786 | 4 | |
| α-helix | 792-817 | 26 | |
| β-strand | 827-832 | 6 | 16 |
| β-strand | 834 | 1 | 17 |
| β-strand | 837 | 1 | 17 |
| α-helix | 839-842 | 4 | |
| α-helix | 849-852 | 4 | |
| β-strand | 857-860 | 4 | 16 |
| β-strand | 870-871 | 2 | 16 |
| β-strand | 874-880 | 7 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoleucyl-tRNA | T | RNA | 75 | Staphylococcus aureus | |
| Isoleucyl-tRNA synthetase | A | protein | 917 | Staphylococcus aureus | P41972 (AlphaFold model) |
>1QU3_1 ISOLEUCYL-TRNA (chains T) GGGCUUGUAGCUCAGGUGGUUAGAGCGCACCCCUGAUAAGGGUGAGGUCGGUGGUUCAAG UCCACUCAGGCCCAC
>1QU3_2 ISOLEUCYL-TRNA SYNTHETASE (chains A) MDYEKTLLMPKTDFPMRGGLPNKEPQIQEKWDAEDQYHKALEKNKGNETFILHDGPPYAN GNLHMGHALNKILKDFIVRYKTMQGFYAPYVPGWDTHGLPIEQALTKKGVDRKKMSTAEF REKCKEFALEQIELQKKDFRRLGVRGDFNDPYITLKPEYEAAQIRIFGEMADKGLIYKGK KPVYWSPSSESSLAEAEIEYHDKRSASIYVAFNVKDDKGVVDADAKFIIWTTTPWTIPSN VAITVHPELKYGQYNVNGEKYIIAEALSDAVAEALDWDKASIKLEKEYTGKELEWVVAQH PFLDRESLVINGDHVTTDAGTGCVHTAPGHGEDDYIVGQQYELPVISPIDDKGVFTEEGG QFEGMFYDKANKAVTDLLTEKGALLKLDFITHSYPHDWRTKKPVIFRATPQWFASISKVR QDILDAIENTNFKVNWGKTRIYNMVRDRGEWVISRQRVWGVPLPVFYAENGEIIMTKETV NHVADLFAEHGSNIWFEREAKDLLPEGFTHPGSPNGTFTKETDIMDVWFDSGSSHRGVLE TRPELSFPADMYLEGSDQYRGWFNSSITTSVATRGVSPYKFLLSHGFVMDGEGKKMSKSL GNVIVPDQVVKQKGADIARLWVSSTDYLADVRISDEILKQTSDDYRKIRNTLRFMLGNIN DFNPDTDSIPESELLEVDRYLLNRLREFTASTINNYENFDYLNIYQEVQNFINVELSNFY LDYGKDILYIEQRDSHIRRSMQTVLYQILVDMTKLLAPILVHTAEEVWSHTPHVKEESVH LADMPKVVEVDQALLDKWRTFMNLRDDVNRALETARNEKVIGKSLEAKVTIASNDKFNAS EFLTSFDALHQLFIVSQVKVVDKLDDQATAYEHGDIVIEHADGEKCERCWNYSEDLGAVD ELTHLCPRCQQVVKSLV
Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. Silvian, L.F., Wang, J., Steitz, T.A. Science (1999) 285:1074-1077. DOI 10.1126/science.285.5430.1074 · PubMed
Other PDB entries of the same protein (UniProt P41972 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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