Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant T84A. Determined by X-ray diffraction at 2.4 Å resolution. Released 4 May 2005.
Explore 2BM0 in 3D Show helices and sheets RCSB PDB PDBe
2BM0 contains 34 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 | 12-19 | 8 | 1 |
| α-helix | 25-36 | 12 | |
| α-helix | 65 | 1 | |
| α-helix | 67 | 1 | |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 91-100 | 10 | |
| β-strand | 103-108 | 6 | 1 |
| α-helix | 118-127 | 10 | |
| β-strand | 132-136 | 5 | 1 |
| β-strand | 138 | 1 | 2 |
| α-helix | 146-155 | 10 | |
| β-strand | 161-163 | 3 | 1 |
| β-strand | 165-168 | 4 | 3 |
| α-helix | 171-173 | 3 | |
| β-strand | 176-179 | 4 | 3 |
| β-strand | 184-188 | 5 | 3 |
| β-strand | 196-199 | 4 | 3 |
| α-helix | 200-201 | 2 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-220 | 15 | |
| α-helix | 221-223 | 3 | |
| α-helix | 225-233 | 9 | |
| α-helix | 235-238 | 4 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 1 |
| β-strand | 262 | 1 | 2 |
| β-strand | 267 | 1 | 2 |
| α-helix | 269-279 | 11 | |
| α-helix | 281-282 | 2 | |
| α-helix | 287-288 | 2 | |
| β-strand | 289-292 | 4 | 4 |
| β-strand | 298-301 | 4 | 4 |
| β-strand | 310-317 | 8 | 5 |
| β-strand | 325-332 | 8 | 5 |
| β-strand | 334-336 | 3 | 6 |
| β-strand | 340-343 | 4 | 5 |
| β-strand | 348-358 | 11 | 5 |
| β-strand | 363-366 | 4 | 5 |
| β-strand | 368-370 | 3 | 6 |
| β-strand | 374-379 | 6 | 5 |
| β-strand | 388-390 | 3 | 5 |
| β-strand | 398 | 1 | 4 |
| α-helix | 401-402 | 2 | |
| β-strand | 409-415 | 7 | 7 |
| α-helix | 419-429 | 11 | |
| α-helix | 431-434 | 4 | |
| 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 | 484-486 | 3 | 8 |
| β-strand | 491-501 | 11 | 9 |
| β-strand | 504-516 | 13 | 9 |
| α-helix | 517-518 | 2 | |
| 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 | 579-596 | 18 | |
| β-strand | 600-612 | 13 | 8 |
| α-helix | 614-616 | 3 | |
| α-helix | 617-626 | 10 | |
| 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 | 681-686 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | THERMUS THERMOPHILUS | P13551 (AlphaFold model) |
>2BM0_1 ELONGATION FACTOR G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIAEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
Structural Insights Into Fusidic Acid Resistance and Sensitivity in EF-G. Hansson, S., Singh, R., Gudkov, A.T. et al. J Mol Biol (2005) 348:939. DOI 10.1016/J.JMB.2005.02.066 · PubMed
Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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