Elongation factor G without nucleotide. Determined by X-ray diffraction at 2.8 Å resolution. Released 1 Aug 1996.
Explore 1ELO in 3D Show helices and sheets RCSB PDB PDBe
1ELO contains 25 α-helices and 60 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 |
|---|---|---|---|
| β-strand | 12-15 | 4 | 1 |
| α-helix | 21-24 | 4 | |
| α-helix | 26-36 | 11 | |
| β-strand | 70-74 | 5 | 1 |
| β-strand | 77-81 | 5 | 1 |
| α-helix | 91-99 | 9 | |
| β-strand | 105-108 | 4 | 2 |
| α-helix | 110-112 | 3 | |
| α-helix | 116-127 | 12 | |
| β-strand | 133-136 | 4 | 2 |
| α-helix | 146-152 | 7 | |
| α-helix | 153-157 | 5 | |
| β-strand | 161 | 1 | 3 |
| β-strand | 165-167 | 3 | 4 |
| β-strand | 177-179 | 3 | 4 |
| β-strand | 184-188 | 5 | 4 |
| β-strand | 196-199 | 4 | 4 |
| α-helix | 200-202 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-223 | 18 | |
| α-helix | 225-231 | 7 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256 | 1 | 3 |
| β-strand | 258-260 | 3 | 2 |
| β-strand | 262 | 1 | 5 |
| α-helix | 263-265 | 3 | |
| β-strand | 267 | 1 | 5 |
| α-helix | 269-279 | 11 | |
| α-helix | 281-282 | 2 | |
| β-strand | 289 | 1 | 6 |
| β-strand | 292 | 1 | 7 |
| β-strand | 298 | 1 | 7 |
| β-strand | 301 | 1 | 6 |
| β-strand | 310-317 | 8 | 8 |
| β-strand | 325-332 | 8 | 8 |
| β-strand | 334-336 | 3 | 9 |
| β-strand | 339-342 | 4 | 10 |
| α-helix | 344-346 | 3 | |
| β-strand | 349-352 | 4 | 10 |
| β-strand | 354-357 | 4 | 8 |
| β-strand | 364-366 | 3 | 8 |
| β-strand | 368-370 | 3 | 9 |
| β-strand | 371 | 1 | 11 |
| β-strand | 373 | 1 | 11 |
| β-strand | 374-378 | 5 | 8 |
| β-strand | 388-389 | 2 | 8 |
| β-strand | 390-391 | 2 | 10 |
| β-strand | 392 | 1 | 12 |
| β-strand | 394 | 1 | 12 |
| α-helix | 395-396 | 2 | |
| β-strand | 398 | 1 | 7 |
| β-strand | 414 | 1 | 13 |
| β-strand | 440 | 1 | 14 |
| β-strand | 451 | 1 | 14 |
| α-helix | 458-463 | 6 | |
| β-strand | 480 | 1 | 13 |
| β-strand | 484-486 | 3 | 15 |
| β-strand | 491-492 | 2 | 16 |
| β-strand | 497-498 | 2 | 17 |
| β-strand | 507-508 | 2 | 17 |
| β-strand | 509-514 | 6 | 16 |
| β-strand | 516 | 1 | 18 |
| β-strand | 519 | 1 | 19 |
| β-strand | 521 | 1 | 19 |
| β-strand | 524-527 | 4 | 16 |
| α-helix | 539-549 | 11 | |
| β-strand | 560 | 1 | 15 |
| β-strand | 563 | 1 | 18 |
| β-strand | 564-571 | 8 | 16 |
| β-strand | 577 | 1 | 17 |
| α-helix | 580-584 | 5 | |
| α-helix | 586-595 | 10 | |
| β-strand | 600-602 | 3 | 15 |
| β-strand | 603-605 | 3 | 20 |
| β-strand | 608-612 | 5 | 21 |
| α-helix | 620-626 | 7 | |
| β-strand | 633-636 | 4 | 21 |
| β-strand | 641-645 | 5 | 21 |
| β-strand | 648 | 1 | 20 |
| α-helix | 655-661 | 7 | |
| β-strand | 668 | 1 | 21 |
| β-strand | 671 | 1 | 21 |
| β-strand | 675-677 | 3 | 20 |
| α-helix | 681-687 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | Thermus thermophilus | Q5SHN5 (AlphaFold model) |
>1ELO_1 ELONGATION FACTOR G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. AEvarsson, A., Brazhnikov, E., Garber, M. et al. EMBO J (1994) 13:3669-3677. PubMed
Other PDB entries of the same protein (UniProt Q5SHN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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