Structure of thermus thermophilus ef-G H573A. Determined by X-ray diffraction at 2.8 Å resolution. Released 22 Nov 2000.
Explore 1FNM in 3D Show helices and sheets RCSB PDB PDBe
1FNM contains 25 α-helices and 42 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 | 9-11 | 3 | |
| β-strand | 12-15 | 4 | 1 |
| β-strand | 17-19 | 3 | 2 |
| α-helix | 25-36 | 12 | |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 91-100 | 10 | |
| β-strand | 104-109 | 6 | 2 |
| β-strand | 113 | 1 | 2 |
| α-helix | 116-127 | 12 | |
| β-strand | 132-137 | 6 | 2 |
| α-helix | 146-152 | 7 | |
| α-helix | 153-157 | 5 | |
| β-strand | 161-163 | 3 | 2 |
| β-strand | 165-168 | 4 | 3 |
| β-strand | 176-179 | 4 | 3 |
| β-strand | 184-188 | 5 | 3 |
| β-strand | 196-197 | 2 | 3 |
| α-helix | 199-202 | 4 | |
| α-helix | 203-221 | 19 | |
| α-helix | 225-233 | 9 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 2 |
| β-strand | 262 | 1 | 4 |
| β-strand | 267 | 1 | 4 |
| α-helix | 269-279 | 11 | |
| α-helix | 287-288 | 2 | |
| β-strand | 289-292 | 4 | 5 |
| β-strand | 298-301 | 4 | 5 |
| β-strand | 310-319 | 10 | 1 |
| β-strand | 323-332 | 10 | 1 |
| β-strand | 334-336 | 3 | 6 |
| β-strand | 339-343 | 5 | 1 |
| β-strand | 348-358 | 11 | 1 |
| β-strand | 363-366 | 4 | 1 |
| β-strand | 368-370 | 3 | 6 |
| β-strand | 374-379 | 6 | 1 |
| β-strand | 388-390 | 3 | 1 |
| β-strand | 398 | 1 | 5 |
| β-strand | 409-415 | 7 | 7 |
| α-helix | 419-434 | 16 | |
| β-strand | 439-442 | 4 | 7 |
| β-strand | 449-453 | 5 | 7 |
| α-helix | 456-467 | 12 | |
| β-strand | 474-476 | 3 | 7 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-481 | 2 | 7 |
| β-strand | 484-486 | 3 | 8 |
| β-strand | 491-499 | 9 | 9 |
| β-strand | 506-516 | 11 | 9 |
| α-helix | 517-518 | 2 | |
| β-strand | 523-527 | 5 | 9 |
| α-helix | 536-538 | 3 | |
| α-helix | 539-549 | 11 | |
| α-helix | 558-559 | 2 | |
| β-strand | 560 | 1 | 8 |
| β-strand | 563-571 | 9 | 9 |
| α-helix | 579-596 | 18 | |
| β-strand | 600-613 | 14 | 8 |
| α-helix | 618-626 | 9 | |
| β-strand | 630-637 | 8 | 8 |
| β-strand | 640-648 | 9 | 8 |
| α-helix | 649-651 | 3 | |
| α-helix | 655-662 | 8 | |
| β-strand | 668-678 | 11 | 8 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-687 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | Thermus thermophilus | P13551 (AlphaFold model) |
>1FNM_1 ELONGATION FACTOR G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYAEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Laurberg, M., Kristensen, O., Martemyanov, K. et al. J Mol Biol (2000) 303:593-603. DOI 10.1006/jmbi.2000.4168 · PubMed
Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1FNM directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.