Crystal structure of elongation factor G mutant(EFG). Determined by X-ray diffraction at 3.0 Å resolution. Released 6 Aug 2014.
Explore 4MYU in 3D Show helices and sheets RCSB PDB PDBe
4MYU contains 27 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 | 9-11 | 3 | |
| β-strand | 12-19 | 8 | 1 |
| α-helix | 25-35 | 11 | |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 91-98 | 8 | |
| β-strand | 103-109 | 7 | 1 |
| β-strand | 113 | 1 | 1 |
| α-helix | 117-127 | 11 | |
| β-strand | 132-137 | 6 | 1 |
| 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 | 196-199 | 4 | 3 |
| α-helix | 200-202 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-220 | 15 | |
| α-helix | 225-231 | 7 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-258 | 3 | 2 |
| β-strand | 259-261 | 3 | 1 |
| β-strand | 262 | 1 | 4 |
| β-strand | 267 | 1 | 4 |
| α-helix | 269-279 | 11 | |
| α-helix | 281-282 | 2 | |
| α-helix | 287-289 | 3 | |
| β-strand | 290-292 | 3 | 5 |
| β-strand | 298-300 | 3 | 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 | 349-358 | 10 | 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 | 421-431 | 11 | |
| β-strand | 439-442 | 4 | 7 |
| β-strand | 449-453 | 5 | 7 |
| α-helix | 456-464 | 9 | |
| α-helix | 465-469 | 5 | |
| β-strand | 474-476 | 3 | 7 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-481 | 2 | 7 |
| β-strand | 484-487 | 4 | 8 |
| β-strand | 491-499 | 9 | 9 |
| β-strand | 506-516 | 11 | 9 |
| β-strand | 523-527 | 5 | 9 |
| α-helix | 536-538 | 3 | |
| α-helix | 539-550 | 12 | |
| β-strand | 560 | 1 | 8 |
| β-strand | 563-571 | 9 | 9 |
| β-strand | 577 | 1 | 9 |
| α-helix | 579-593 | 15 | |
| β-strand | 599-613 | 15 | 8 |
| α-helix | 614-616 | 3 | |
| α-helix | 617-625 | 9 | |
| β-strand | 633-637 | 5 | 8 |
| β-strand | 640-645 | 6 | 8 |
| β-strand | 648 | 1 | 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) |
>4MYU_1 Elongation factor G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYKEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
Crystal structure of elongation factor G mutant(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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