Crystal structure of elongation factor G (EFG). Determined by X-ray diffraction at 3.5 Å resolution. Released 6 Aug 2014.
Explore 4MYT in 3D Show helices and sheets RCSB PDB PDBe
4MYT contains 24 α-helices and 52 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 | 15 | 1 | 1 |
| β-strand | 17-19 | 3 | 2 |
| α-helix | 25-36 | 12 | |
| β-strand | 69-70 | 2 | 1 |
| β-strand | 73-74 | 2 | 3 |
| β-strand | 77-78 | 2 | 3 |
| β-strand | 81-82 | 2 | 1 |
| α-helix | 83-84 | 2 | |
| α-helix | 88-90 | 3 | |
| α-helix | 92-100 | 9 | |
| β-strand | 105-109 | 5 | 2 |
| α-helix | 116-127 | 12 | |
| β-strand | 133-137 | 5 | 2 |
| α-helix | 146-157 | 12 | |
| β-strand | 162-163 | 2 | 2 |
| β-strand | 165-167 | 3 | 4 |
| β-strand | 176-179 | 4 | 4 |
| β-strand | 184-187 | 4 | 4 |
| β-strand | 197-199 | 3 | 4 |
| α-helix | 206-220 | 15 | |
| α-helix | 225-232 | 8 | |
| α-helix | 239-251 | 13 | |
| β-strand | 257-260 | 4 | 2 |
| β-strand | 262 | 1 | 5 |
| β-strand | 267 | 1 | 5 |
| α-helix | 269-278 | 10 | |
| α-helix | 281-282 | 2 | |
| α-helix | 287-288 | 2 | |
| β-strand | 289-290 | 2 | 6 |
| β-strand | 292 | 1 | 7 |
| β-strand | 300-301 | 2 | 6 |
| β-strand | 310-318 | 9 | 8 |
| β-strand | 324-332 | 9 | 8 |
| β-strand | 335-336 | 2 | 9 |
| β-strand | 340-343 | 4 | 8 |
| β-strand | 349-356 | 8 | 8 |
| β-strand | 365-366 | 2 | 8 |
| β-strand | 368-369 | 2 | 9 |
| β-strand | 374-379 | 6 | 8 |
| β-strand | 388-391 | 4 | 8 |
| β-strand | 398 | 1 | 7 |
| β-strand | 409-415 | 7 | 10 |
| α-helix | 422-433 | 12 | |
| β-strand | 439-442 | 4 | 10 |
| β-strand | 449-453 | 5 | 10 |
| α-helix | 457-466 | 10 | |
| β-strand | 474-476 | 3 | 10 |
| β-strand | 480-481 | 2 | 10 |
| β-strand | 484-486 | 3 | 11 |
| β-strand | 491 | 1 | 12 |
| β-strand | 494-495 | 2 | 12 |
| β-strand | 498 | 1 | 13 |
| β-strand | 507 | 1 | 13 |
| β-strand | 509-516 | 8 | 12 |
| α-helix | 517-518 | 2 | |
| β-strand | 523-527 | 5 | 12 |
| α-helix | 536-538 | 3 | |
| α-helix | 539-549 | 11 | |
| β-strand | 560 | 1 | 11 |
| β-strand | 563-571 | 9 | 12 |
| β-strand | 577 | 1 | 13 |
| α-helix | 583-594 | 12 | |
| β-strand | 600-605 | 6 | 11 |
| β-strand | 608-612 | 5 | 14 |
| α-helix | 617-624 | 8 | |
| β-strand | 634-637 | 4 | 14 |
| β-strand | 640-645 | 6 | 14 |
| β-strand | 648 | 1 | 11 |
| α-helix | 649-651 | 3 | |
| α-helix | 655-660 | 6 | |
| β-strand | 668 | 1 | 14 |
| β-strand | 671 | 1 | 14 |
| β-strand | 675-678 | 4 | 11 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-686 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | Thermus thermophilus | P13551 (AlphaFold model) |
>4MYT_1 Elongation factor G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSAMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
Crystal structure of elongation factor G (EFG). Liu, G., Dong, J., Gong, W. et al. To be published.
Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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