E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 7 Dec 1998.
Explore 1B23 in 3D Show helices and sheets RCSB PDB PDBe
1B23 contains 16 α-helices and 28 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 |
|---|---|---|---|
| β-strand | 4 | 1 | 1 |
| β-strand | 11-17 | 7 | 2 |
| α-helix | 24-38 | 15 | |
| α-helix | 47-50 | 4 | |
| α-helix | 54-59 | 6 | |
| β-strand | 66-71 | 6 | 2 |
| β-strand | 76-81 | 6 | 2 |
| α-helix | 82-83 | 2 | |
| α-helix | 86-88 | 3 | |
| α-helix | 89-96 | 8 | |
| β-strand | 101-107 | 7 | 2 |
| α-helix | 114-125 | 12 | |
| β-strand | 130-136 | 7 | 2 |
| α-helix | 138-140 | 3 | |
| α-helix | 144-160 | 17 | |
| β-strand | 170-172 | 3 | 2 |
| α-helix | 175-184 | 10 | |
| α-helix | 194-209 | 16 | |
| α-helix | 213-215 | 3 | |
| α-helix | 220-221 | 2 | |
| β-strand | 222-224 | 3 | 3 |
| β-strand | 227-231 | 5 | 4 |
| β-strand | 235-241 | 7 | 4 |
| β-strand | 244 | 1 | 3 |
| β-strand | 246-248 | 3 | 5 |
| β-strand | 252-256 | 5 | 3 |
| β-strand | 264-266 | 3 | 3 |
| β-strand | 267-270 | 4 | 4 |
| β-strand | 271-272 | 2 | 1 |
| β-strand | 275-276 | 2 | 1 |
| β-strand | 279-281 | 3 | 5 |
| β-strand | 285-290 | 6 | 4 |
| β-strand | 303-305 | 3 | 3 |
| β-strand | 313-322 | 10 | 6 |
| α-helix | 323-324 | 2 | |
| α-helix | 325-327 | 3 | |
| β-strand | 334 | 1 | 7 |
| β-strand | 341-344 | 4 | 6 |
| β-strand | 347-354 | 8 | 6 |
| α-helix | 355-356 | 2 | |
| β-strand | 362 | 1 | 7 |
| β-strand | 367-378 | 12 | 6 |
| β-strand | 385-390 | 6 | 6 |
| β-strand | 393-402 | 10 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cysteinyl tRNA | R | RNA | 74 | Escherichia coli | |
| Elongation factor tu | P | protein | 405 | Thermus aquaticus | Q01698 (AlphaFold model) |
>1B23_1 CYSTEINYL TRNA (chains R) GGCGCGUUAACAAAGCGGUUAUGUAGCGGAUUGCAAAUCCGUCUAGUCCGGUUCGACUCC GGAACGCGCCUCCA
>1B23_2 ELONGATION FACTOR TU (chains P) AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDIDKAPEERARG ITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREHI LLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFPGDEVPVIRGSALLALE EMHKNPKTKRGENEWVDKIWELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATG RIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVTGVVRLPQGVE MVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 3 |
| CYS | Cysteine | C3 H7 N O2 S | 1 |
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 1 |
Water and common crystallization additives (SO4) are not listed.
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Nissen, P., Thirup, S., Kjeldgaard, M. et al. Structure (1999) 7:143-156. DOI 10.1016/S0969-2126(99)80021-5 · 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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