Insights into editing from an ile-tRNA synthetase structure with trna(ile) and mupirocin. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Aug 2000.
Explore 1FFY in 3D Show helices and sheets RCSB PDB PDBe
1FFY contains 50 α-helices and 44 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 | 4-6 | 3 | |
| α-helix | 20-33 | 14 | |
| α-helix | 36-43 | 8 | |
| β-strand | 49 | 1 | 1 |
| β-strand | 52-53 | 2 | 2 |
| α-helix | 54-55 | 2 | |
| β-strand | 58 | 1 | 3 |
| α-helix | 65-82 | 18 | |
| β-strand | 87 | 1 | 1 |
| β-strand | 93-94 | 2 | 4 |
| β-strand | 95 | 1 | 3 |
| α-helix | 99-108 | 10 | |
| α-helix | 117-140 | 24 | |
| β-strand | 152-153 | 2 | 4 |
| α-helix | 157-172 | 16 | |
| β-strand | 176-186 | 11 | 5 |
| β-strand | 191-192 | 2 | 5 |
| α-helix | 195-197 | 3 | |
| β-strand | 198-207 | 10 | 6 |
| β-strand | 208-209 | 2 | 7 |
| β-strand | 212 | 1 | 8 |
| β-strand | 221-224 | 4 | 9 |
| β-strand | 227 | 1 | 8 |
| β-strand | 230-231 | 2 | 7 |
| α-helix | 234-236 | 3 | |
| β-strand | 241 | 1 | 10 |
| α-helix | 265-272 | 8 | |
| β-strand | 299 | 1 | 11 |
| β-strand | 307 | 1 | 11 |
| β-strand | 326 | 1 | 10 |
| α-helix | 333-336 | 4 | |
| α-helix | 344-346 | 3 | |
| α-helix | 369 | 1 | |
| α-helix | 370-374 | 5 | |
| α-helix | 375-377 | 3 | |
| α-helix | 380-383 | 4 | |
| β-strand | 388-397 | 10 | 6 |
| β-strand | 403 | 1 | 6 |
| β-strand | 405-414 | 10 | 5 |
| α-helix | 416-428 | 13 | |
| β-strand | 431-432 | 2 | 2 |
| α-helix | 435-447 | 13 | |
| β-strand | 451-452 | 2 | 5 |
| β-strand | 454-455 | 2 | 12 |
| α-helix | 461 | 1 | |
| β-strand | 462 | 1 | 12 |
| α-helix | 463 | 1 | |
| β-strand | 466-467 | 2 | 13 |
| β-strand | 473-474 | 2 | 13 |
| α-helix | 477-490 | 14 | |
| α-helix | 493-497 | 5 | |
| α-helix | 500-503 | 4 | |
| β-strand | 519-520 | 2 | 13 |
| β-strand | 524-525 | 2 | 12 |
| α-helix | 527-532 | 6 | |
| α-helix | 534 | 1 | |
| α-helix | 535-540 | 6 | |
| β-strand | 549 | 1 | 14 |
| β-strand | 551-555 | 5 | 2 |
| α-helix | 556-559 | 4 | |
| α-helix | 562-574 | 13 | |
| β-strand | 579 | 1 | 14 |
| β-strand | 581-585 | 5 | 2 |
| β-strand | 588-589 | 2 | 15 |
| α-helix | 606-612 | 7 | |
| α-helix | 615-623 | 9 | |
| β-strand | 631-632 | 2 | 15 |
| α-helix | 635-657 | 23 | |
| α-helix | 664-667 | 4 | |
| α-helix | 668-670 | 3 | |
| α-helix | 671-673 | 3 | |
| α-helix | 676-697 | 22 | |
| α-helix | 701-710 | 10 | |
| α-helix | 711-721 | 11 | |
| α-helix | 722-728 | 7 | |
| α-helix | 736-756 | 21 | |
| α-helix | 761-768 | 8 | |
| α-helix | 779-781 | 3 | |
| α-helix | 783-787 | 5 | |
| α-helix | 792-817 | 26 | |
| α-helix | 824-826 | 3 | |
| β-strand | 827-832 | 6 | 16 |
| α-helix | 839-842 | 4 | |
| α-helix | 843-845 | 3 | |
| α-helix | 849-852 | 4 | |
| β-strand | 857-860 | 4 | 16 |
| β-strand | 869-871 | 3 | 16 |
| β-strand | 874-880 | 7 | 16 |
| α-helix | 881 | 1 | |
| β-strand | 884-885 | 2 | 17 |
| β-strand | 892-893 | 2 | 17 |
| β-strand | 897-899 | 3 | 18 |
| β-strand | 902-905 | 4 | 18 |
| α-helix | 907-914 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoleucyl-tRNA | T | RNA | 75 | ||
| Isoleucyl-tRNA synthetase | A | protein | 917 | Staphylococcus aureus | P41972 (AlphaFold model) |
>1FFY_1 ISOLEUCYL-TRNA (chains T) GGGCUUGUAGCUCAGGUGGUUAGAGCGCACCCCUGAUAAGGGUGAGGUCGGUGGUUCAAG UCCACUCAGGCCCAC
>1FFY_2 ISOLEUCYL-TRNA SYNTHETASE (chains A) MDYEKTLLMPKTDFPMRGGLPNKEPQIQEKWDAEDQYHKALEKNKGNETFILHDGPPYAN GNLHMGHALNKILKDFIVRYKTMQGFYAPYVPGWDTHGLPIEQALTKKGVDRKKMSTAEF REKCKEFALEQIELQKKDFRRLGVRGDFNDPYITLKPEYEAAQIRIFGEMADKGLIYKGK KPVYWSPSSESSLAEAEIEYHDKRSASIYVAFNVKDDKGVVDADAKFIIWTTTPWTIPSN VAITVHPELKYGQYNVNGEKYIIAEALSDAVAEALDWDKASIKLEKEYTGKELEWVVAQH PFLDRESLVINGDHVTTDAGTGCVHTAPGHGEDDYIVGQQYELPVISPIDDKGVFTEEGG QFEGMFYDKANKAVTDLLTEKGALLKLDFITHSYPHDWRTKKPVIFRATPQWFASISKVR QDILDAIENTNFKVNWGKTRIYNMVRDRGEWVISRQRVWGVPLPVFYAENGEIIMTKETV NHVADLFAEHGSNIWFEREAKDLLPEGFTHPGSPNGTFTKETDIMDVWFDSGSSHRGVLE TRPELSFPADMYLEGSDQYRGWFNSSITTSVATRGVSPYKFLLSHGFVMDGEGKKMSKSL GNVIVPDQVVKQKGADIARLWVSSTDYLADVRISDEILKQTSDDYRKIRNTLRFMLGNIN DFNPDTDSIPESELLEVDRYLLNRLREFTASTINNYENFDYLNIYQEVQNFINVELSNFY LDYGKDILYIEQRDSHIRRSMQTVLYQILVDMTKLLAPILVHTAEEVWSHTPHVKEESVH LADMPKVVEVDQALLDKWRTFMNLRDDVNRALETARNEKVIGKSLEAKVTIASNDKFNAS EFLTSFDALHQLFIVSQVKVVDKLDDQATAYEHGDIVIEHADGEKCERCWNYSEDLGAVD ELTHLCPRCQQVVKSLV
Water and common crystallization additives (K) are not listed.
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:
1FFY is part of these collections:
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