Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant G16V. Determined by X-ray diffraction at 2.6 Å resolution. Released 4 May 2005.
Explore 2BM1 in 3D Show helices and sheets RCSB PDB PDBe
2BM1 contains 30 α-helices and 46 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 | 25-37 | 13 | |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 83 | 1 | |
| α-helix | 93-100 | 8 | |
| β-strand | 103-109 | 7 | 1 |
| β-strand | 113 | 1 | 1 |
| α-helix | 118-127 | 10 | |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 146-157 | 12 | |
| β-strand | 161-163 | 3 | 1 |
| β-strand | 165-168 | 4 | 2 |
| α-helix | 171-173 | 3 | |
| β-strand | 176-179 | 4 | 2 |
| β-strand | 184-188 | 5 | 2 |
| β-strand | 196-199 | 4 | 2 |
| α-helix | 200-202 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-221 | 16 | |
| α-helix | 225-231 | 7 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 1 |
| β-strand | 262 | 1 | 3 |
| β-strand | 267 | 1 | 3 |
| α-helix | 269-279 | 11 | |
| α-helix | 281-282 | 2 | |
| α-helix | 283-285 | 3 | |
| α-helix | 287-289 | 3 | |
| β-strand | 290-292 | 3 | 4 |
| β-strand | 298-300 | 3 | 4 |
| β-strand | 310-317 | 8 | 1 |
| β-strand | 325-332 | 8 | 1 |
| β-strand | 334-336 | 3 | 5 |
| β-strand | 340-343 | 4 | 1 |
| β-strand | 348-358 | 11 | 1 |
| β-strand | 363-365 | 3 | 1 |
| β-strand | 368-370 | 3 | 5 |
| β-strand | 374-379 | 6 | 1 |
| β-strand | 388-390 | 3 | 1 |
| β-strand | 398 | 1 | 4 |
| β-strand | 409-411 | 3 | 6 |
| β-strand | 412-413 | 2 | 7 |
| β-strand | 414 | 1 | 8 |
| α-helix | 425-427 | 3 | |
| α-helix | 431-433 | 3 | |
| β-strand | 439-441 | 3 | 7 |
| β-strand | 449-452 | 4 | 7 |
| β-strand | 453 | 1 | 6 |
| α-helix | 456-460 | 5 | |
| α-helix | 463-465 | 3 | |
| β-strand | 475 | 1 | 8 |
| β-strand | 479-481 | 3 | 6 |
| β-strand | 484-486 | 3 | 9 |
| β-strand | 491-500 | 10 | 10 |
| β-strand | 505-516 | 12 | 10 |
| α-helix | 517-518 | 2 | |
| β-strand | 523-527 | 5 | 10 |
| α-helix | 539-550 | 12 | |
| β-strand | 560 | 1 | 9 |
| β-strand | 563-571 | 9 | 10 |
| β-strand | 577 | 1 | 10 |
| α-helix | 579-596 | 18 | |
| β-strand | 600-613 | 14 | 9 |
| α-helix | 614-616 | 3 | |
| α-helix | 617-623 | 7 | |
| α-helix | 625-627 | 3 | |
| β-strand | 631-637 | 7 | 9 |
| β-strand | 640-648 | 9 | 9 |
| α-helix | 649-652 | 4 | |
| α-helix | 656-659 | 4 | |
| β-strand | 668 | 1 | 9 |
| β-strand | 672-678 | 7 | 9 |
| α-helix | 681-686 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | THERMUS THERMOPHILUS | P13551 (AlphaFold model) |
>2BM1_1 ELONGATION FACTOR G (chains A) MAVKVEYDLKRLRNIVIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET 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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