Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors. Determined by electron microscopy at 7.3 Å resolution. Released 15 Jan 2008.
Explore 2OM7 in 3D Show helices and sheets RCSB PDB PDBe
2OM7 contains 41 α-helices and 57 β-strands across 4 chains. 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 | 7-12 | 6 | |
| β-strand | 33-40 | 8 | 1 |
| β-strand | 55-60 | 6 | 1 |
| β-strand | 65-69 | 5 | 1 |
| β-strand | 82-85 | 4 | 1 |
| β-strand | 99-100 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-25 | 3 | |
| β-strand | 43 | 1 | 2 |
| α-helix | 58-59 | 2 | |
| α-helix | 191-195 | 5 | |
| β-strand | 212-213 | 2 | 2 |
| β-strand | 218-219 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| β-strand | 12-19 | 8 | 3 |
| α-helix | 25-36 | 12 | |
| β-strand | 69-74 | 6 | 3 |
| β-strand | 77-82 | 6 | 3 |
| α-helix | 91-100 | 10 | |
| β-strand | 103-109 | 7 | 3 |
| β-strand | 113 | 1 | 3 |
| α-helix | 116-127 | 12 | |
| β-strand | 132-137 | 6 | 3 |
| α-helix | 146-152 | 7 | |
| α-helix | 153-157 | 5 | |
| β-strand | 161-163 | 3 | 3 |
| β-strand | 165-168 | 4 | 4 |
| β-strand | 176-179 | 4 | 4 |
| β-strand | 184-188 | 5 | 4 |
| β-strand | 196-197 | 2 | 4 |
| α-helix | 199-202 | 4 | |
| α-helix | 203-221 | 19 | |
| α-helix | 225-233 | 9 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 3 |
| β-strand | 262 | 1 | 5 |
| β-strand | 267 | 1 | 5 |
| α-helix | 269-279 | 11 | |
| α-helix | 287-288 | 2 | |
| β-strand | 289-292 | 4 | 6 |
| β-strand | 298-301 | 4 | 6 |
| β-strand | 310-319 | 10 | 3 |
| β-strand | 323-332 | 10 | 3 |
| β-strand | 334-336 | 3 | 7 |
| β-strand | 339-343 | 5 | 3 |
| β-strand | 348-358 | 11 | 3 |
| β-strand | 363-366 | 4 | 3 |
| β-strand | 368-370 | 3 | 7 |
| β-strand | 374-379 | 6 | 3 |
| β-strand | 388-390 | 3 | 3 |
| β-strand | 398 | 1 | 6 |
| β-strand | 409-415 | 7 | 8 |
| α-helix | 419-434 | 16 | |
| β-strand | 439-442 | 4 | 8 |
| β-strand | 449-453 | 5 | 8 |
| α-helix | 456-467 | 12 | |
| β-strand | 474-476 | 3 | 8 |
| α-helix | 477-479 | 3 | |
| β-strand | 480-482 | 3 | 8 |
| β-strand | 491-499 | 9 | 9 |
| β-strand | 506-516 | 11 | 9 |
| α-helix | 517-518 | 2 | |
| β-strand | 523-527 | 5 | 9 |
| α-helix | 536-538 | 3 | |
| α-helix | 539-549 | 11 | |
| α-helix | 558-560 | 3 | |
| β-strand | 563-571 | 9 | 9 |
| α-helix | 579-596 | 18 | |
| β-strand | 602-613 | 12 | 10 |
| α-helix | 618-626 | 9 | |
| β-strand | 630-634 | 5 | 10 |
| β-strand | 637 | 1 | 10 |
| β-strand | 640-648 | 9 | 10 |
| α-helix | 649-651 | 3 | |
| β-strand | 653-654 | 2 | 8 |
| α-helix | 655-662 | 8 | |
| β-strand | 668-678 | 11 | 10 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-687 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-15 | 8 | |
| β-strand | 19 | 1 | 11 |
| α-helix | 26-30 | 5 | |
| β-strand | 34-36 | 3 | 11 |
| β-strand | 39-41 | 3 | 11 |
| α-helix | 44-62 | 19 | |
| β-strand | 69-71 | 3 | 12 |
| α-helix | 75-77 | 3 | |
| α-helix | 78-86 | 9 | |
| β-strand | 92-93 | 2 | 12 |
| α-helix | 102-104 | 3 | |
| α-helix | 105-122 | 18 | |
| α-helix | 125-128 | 4 | |
| α-helix | 132-149 | 18 | |
| β-strand | 162-164 | 3 | 12 |
| α-helix | 168-170 | 3 | |
| α-helix | 171-179 | 9 | |
| β-strand | 184-188 | 5 | 12 |
| β-strand | 199-202 | 4 | 12 |
| α-helix | 208-224 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fragment of 16S rRNA (h14) | A | RNA | 12 | Thermus thermophilus | |
| Fragment of 16S rRNA (h15) | B | RNA | 28 | Thermus thermophilus | |
| Fragment of 16S rRNA (h44) | C | RNA | 96 | Thermus thermophilus | |
| 16S ribosomal RNA (H5) | D | RNA | 303 | Thermus thermophilus | |
| Fragment of23S rRNA (H95) | F | RNA | 29 | Thermus thermophilus | |
| Fragment of23S rRNA (H68) | G | RNA | 54 | Thermus thermophilus | |
| Fragment of23S rRNA (H89) | H | RNA | 42 | Thermus thermophilus | |
| Fragment of23S rRNA (H42-44) | I | RNA | 58 | Thermus thermophilus | |
| Fragment of23S rRNA (H76) | J | RNA | 102 | Thermus thermophilus | |
| p/E-tRNA | M | RNA | 74 | Thermus thermophilus | |
| 30S ribosomal protein S12 | E | protein | 135 | Thermus thermophilus | Q5SHN3 (AlphaFold model) |
| 50S ribosomal protein L1 | K | protein | 229 | Thermus thermophilus | Q5SLP7 (AlphaFold model) |
2 more molecules are not listed.
>2OM7_1 Fragment of 16S rRNA (h14) (chains A) CUCCUACGGGAG
>2OM7_2 Fragment of 16S rRNA (h15) (chains B) UUCCGCAAUGGGCGCAAGCCUGACGGAG
>2OM7_3 Fragment of 16S rRNA (h44) (chains C) GCCCGUCACGCCAUGGGAGCGGGCUCUACCCGAAGUCGCCGGGAGCCUACGGGCAGGCGC CGAGGGUAGGGCCCGUGACUGGGGCGAAGUCGUAAC
>2OM7_4 16S ribosomal RNA (H5) (chains D) GACAUGCAAGUCGUGCGGGCCGCGGGGUUUUACUCCGUGGUCAGCGGCGGACGGGUGAGU AACGCGUGGGUGACCUACCCGGAAGAGGGGGACAACCCGGGGAAACUCGGGCUAAUCCCC CAUGUGGACCCGCCCCUUGGGGUGUGUCCAAAGGGCUUUGCCCGCUUCCGGAUGGGCCCG CGUCCCAUCAGCUAGUUGGUGGGGUAAUGGCCCACCAAGGCGACGACGGGUAGCCGGUCU GAGAGGAUGGCCGGCCACAGGGGCACUGAGACACGGGCCCCACUCCUACGGGAGGCAGCA GUU
>2OM7_5 Fragment of23S rRNA (H95) (chains F) CUCUUCCUAGUACGAGAGGACCGGAAGGG
>2OM7_6 Fragment of23S rRNA (H68) (chains G) GUGCCGGAAGGUCAAGGGGAGGGGUGCAAGCCCCGAACCGAAGCCCCGGUGAAC
>2OM7_7 Fragment of23S rRNA (H89) (chains H) GCUGAUCUCCCCCGAGCGUCCACAGCGGCGGGGAGGUUUGGC
>2OM7_8 Fragment of23S rRNA (H42-44) (chains I) GCCAGGAGGUUGGCUUAGAAGCAGCCAUCCUUUAAAGAGUGCGUAAUAGCUCACUGGU
>2OM7_9 Fragment of23S rRNA (H76) (chains J) GCUCUUGGUCGCGCCUGCGUAGGAUAGGUGGGAGCCUGUGAACCCCCGCCUCCGGGUGGG GGGGAGGCGCCGGUGAAAUACCACCCUGGCGCGGCUGGGGGC
>2OM7_10 p/E-tRNA (chains M) UCCGUGAUAACAAAGCGGUUAUGUACCGGAUUUUUAUUCCGGCUAUCGGGGUUCAAUUCC CCGUCGCGGAGCCA
>2OM7_11 30S ribosomal protein S12 (chains E) MVALPTINQLVRKGREKVRKKSKVPALKGAPFRRGVCTVVRTVTPKKPNSALRKVAKVRL TSGYEVTAYIPGEGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGVYDAAGVKDRKKSRSKY GTKKPKEAAKTAAKK
>2OM7_12 50S ribosomal protein L1 (chains K) MPKHGKRYRALLEKVDPNKVYTIDEAARLVKELATAKFDETVEVHAKLGIDPRRSDQNVR GTVSLPHGLGKQVRVLAIAKGEKIKEAEEAGADYVGGEEIIQKILDGWMDFDAVVATPDV MGAVGSKLGRILGPRGLLPNPKAGTVGFNIGEIIREIKAGRIEFRNDKTGAIHAPVGKAS FPPEKLADNIRAFIRALEAHKPEGAKGTFLRSVYVTTTMGPSVRINPHS
Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors. Connell, S.R., Takemoto, C., Wilson, D.N. et al. Mol Cell (2007) 25:751-764. DOI 10.1016/j.molcel.2007.01.027 · PubMed
Other PDB entries of the same protein (UniProt Q5SHN3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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