ef-tu (Escherichia coli) complexed with nvp-ldu796. Determined by X-ray diffraction at 2.3 Å resolution. Released 26 Dec 2012.
Explore 4G5G in 3D Show helices and sheets RCSB PDB PDBe
4G5G contains 13 α-helices and 33 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 | 11-15 | 5 | 1 |
| β-strand | 16-17 | 2 | 2 |
| α-helix | 24-39 | 16 | |
| α-helix | 46-50 | 5 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54-56 | 3 | 3 |
| β-strand | 61-63 | 3 | 3 |
| β-strand | 65-70 | 6 | 1 |
| β-strand | 75-80 | 6 | 1 |
| α-helix | 84-93 | 10 | |
| β-strand | 101-106 | 6 | 2 |
| α-helix | 113-125 | 13 | |
| β-strand | 130-135 | 6 | 2 |
| α-helix | 145-159 | 15 | |
| β-strand | 169-171 | 3 | 2 |
| α-helix | 174-178 | 5 | |
| α-helix | 182-198 | 17 | |
| α-helix | 200-204 | 5 | |
| α-helix | 205-207 | 3 | |
| α-helix | 209-210 | 2 | |
| β-strand | 211-213 | 3 | 4 |
| β-strand | 217-220 | 4 | 5 |
| β-strand | 224-230 | 7 | 5 |
| β-strand | 233 | 1 | 4 |
| β-strand | 235-237 | 3 | 6 |
| β-strand | 241-245 | 5 | 4 |
| β-strand | 251-254 | 4 | 4 |
| β-strand | 255-260 | 6 | 5 |
| β-strand | 263-265 | 3 | 5 |
| β-strand | 267-269 | 3 | 6 |
| β-strand | 273-278 | 6 | 5 |
| β-strand | 288 | 1 | 7 |
| β-strand | 290 | 1 | 7 |
| β-strand | 291-293 | 3 | 4 |
| β-strand | 299-310 | 12 | 8 |
| α-helix | 311-312 | 2 | |
| β-strand | 322-323 | 2 | 9 |
| β-strand | 324 | 1 | 10 |
| β-strand | 326 | 1 | 10 |
| β-strand | 329-332 | 4 | 8 |
| β-strand | 335-342 | 8 | 8 |
| α-helix | 343 | 1 | |
| β-strand | 349-350 | 2 | 9 |
| β-strand | 355-368 | 14 | 8 |
| β-strand | 373-378 | 6 | 8 |
| β-strand | 381-391 | 11 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor Tu 1 | A | protein | 394 | Escherichia coli | P0CE47 (AlphaFold model) |
| thiomuracin A derivative | I | protein | 13 | synthetic construct |
>4G5G_1 Elongation factor Tu 1 (chains A) MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
>4G5G_2 thiomuracin A derivative (chains I) SCNCFCYPCCSCX
Water and common crystallization additives (SO4) are not listed.
Antibiotic optimization and chemical structure stabilization of thiomuracin A. LaMarche, M.J., Leeds, J.A., Dzink-Fox, J. et al. J Med Chem (2012) 55:6934-6941. DOI 10.1021/jm300783c · PubMed
Other PDB entries of the same protein (UniProt P0CE47 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4G5G directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.