T. aquaticus elongation factor EF-Tu complexed with the antibiotic enacyloxin IIa, a GTP analog, and Phe-tRNA. Determined by X-ray diffraction at 3.1 Å resolution. Released 13 Oct 2005.
Explore 1OB5 in 3D Show helices and sheets RCSB PDB PDBe
1OB5 contains 48 α-helices and 87 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 11-16 | 6 | 1 |
| α-helix | 26-32 | 7 | |
| α-helix | 47-50 | 4 | |
| α-helix | 54-55 | 2 | |
| α-helix | 56-60 | 5 | |
| β-strand | 66-67 | 2 | 1 |
| β-strand | 70-71 | 2 | 1 |
| β-strand | 76-81 | 6 | 1 |
| α-helix | 86-88 | 3 | |
| α-helix | 89-95 | 7 | |
| β-strand | 102-107 | 6 | 1 |
| α-helix | 114-125 | 12 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 138-140 | 3 | |
| α-helix | 144-147 | 4 | |
| α-helix | 152-160 | 9 | |
| β-strand | 170 | 1 | 1 |
| α-helix | 177-184 | 8 | |
| α-helix | 195-209 | 15 | |
| β-strand | 223-224 | 2 | 2 |
| β-strand | 229 | 1 | 3 |
| β-strand | 237-239 | 3 | 3 |
| β-strand | 247-248 | 2 | 4 |
| β-strand | 252-255 | 4 | 2 |
| β-strand | 263-266 | 4 | 2 |
| β-strand | 279-280 | 2 | 4 |
| β-strand | 287-289 | 3 | 3 |
| α-helix | 295-297 | 3 | |
| β-strand | 303-304 | 2 | 2 |
| β-strand | 312-313 | 2 | 5 |
| β-strand | 317-322 | 6 | 6 |
| α-helix | 323-324 | 2 | |
| α-helix | 325-327 | 3 | |
| β-strand | 334 | 1 | 7 |
| α-helix | 340 | 1 | |
| β-strand | 341-343 | 3 | 6 |
| β-strand | 348-350 | 3 | 6 |
| β-strand | 351 | 1 | 8 |
| β-strand | 354 | 1 | 6 |
| β-strand | 362 | 1 | 7 |
| β-strand | 367-371 | 5 | 6 |
| β-strand | 374 | 1 | 8 |
| β-strand | 378-379 | 2 | 5 |
| β-strand | 386-390 | 5 | 6 |
| β-strand | 393-399 | 7 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor tu | A, C, E | protein | 405 | THERMUS AQUATICUS | Q01698 (AlphaFold model) |
| Transfer-RNA, phe | B, D, F | RNA | 78 | SACCHAROMYCES CEREVISIAE |
>1OB5_1 ELONGATION FACTOR TU (chains A, C, E) AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDIDKAPEERARG ITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREHI LLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFPGDEVPVIRGSALLALE EMHKNPKTKRGENEWVDKIWELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATG RIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVTGVVRLPQGVE MVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE
>1OB5_2 TRANSFER-RNA, PHE (chains B, D, F) GCGGAUUUAGCUCAGUUGGGAGAGCGCCAGACUGAAGAUCUGGAGGUCCUGUGUUCGAUC CACAGAAUUCGCACCAFC
| ID | Name | Formula | Copies |
|---|---|---|---|
| ENX | Enacyloxin iia | C33 H45 Cl2 N O11 | 3 |
| MG | Magnesium ion | Mg | 3 |
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 3 |
Enacyloxin Iia Pinpoints a Binding Pocket of Elongation Factor TU for Development of Novel Antibiotics. Parmeggiani, A., Krab, I.M., Watanabe, T. et al. J Biol Chem (2006) 281:2893. DOI 10.1074/JBC.M505951200 · PubMed
Other PDB entries of the same protein (UniProt Q01698 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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