Ef-tu (escherichia coli) in complex with nvp-ldk733. Determined by X-ray diffraction at 2.45 Å resolution. Released 8 Feb 2012.
Explore 3U6K in 3D Show helices and sheets RCSB PDB PDBe
3U6K contains 31 α-helices and 60 β-strands across 2 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 | 11-17 | 7 | 1 |
| α-helix | 24-38 | 15 | |
| α-helix | 46-50 | 5 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54-57 | 4 | 2 |
| β-strand | 60-63 | 4 | 2 |
| β-strand | 65-70 | 6 | 1 |
| β-strand | 75-80 | 6 | 1 |
| α-helix | 84-93 | 10 | |
| β-strand | 100-106 | 7 | 1 |
| α-helix | 113-124 | 12 | |
| β-strand | 130-135 | 6 | 1 |
| α-helix | 137-139 | 3 | |
| α-helix | 145-159 | 15 | |
| α-helix | 164-166 | 3 | |
| β-strand | 169-171 | 3 | 1 |
| α-helix | 174-179 | 6 | |
| α-helix | 184-198 | 15 | |
| α-helix | 200-204 | 5 | |
| α-helix | 205-207 | 3 | |
| α-helix | 209-210 | 2 | |
| β-strand | 211-213 | 3 | 3 |
| β-strand | 217-220 | 4 | 4 |
| β-strand | 224-230 | 7 | 4 |
| β-strand | 233 | 1 | 3 |
| β-strand | 235-237 | 3 | 5 |
| β-strand | 241-246 | 6 | 3 |
| β-strand | 248-254 | 7 | 3 |
| β-strand | 255-260 | 6 | 4 |
| β-strand | 263-265 | 3 | 4 |
| β-strand | 267-269 | 3 | 5 |
| β-strand | 273-278 | 6 | 4 |
| α-helix | 283-285 | 3 | |
| β-strand | 288 | 1 | 6 |
| β-strand | 290 | 1 | 6 |
| β-strand | 291-293 | 3 | 3 |
| β-strand | 300-310 | 11 | 7 |
| α-helix | 311-312 | 2 | |
| α-helix | 313-315 | 3 | |
| α-helix | 321 | 1 | |
| β-strand | 322-323 | 2 | 8 |
| β-strand | 329-332 | 4 | 7 |
| β-strand | 335-342 | 8 | 7 |
| α-helix | 343 | 1 | |
| β-strand | 349-350 | 2 | 8 |
| β-strand | 355-367 | 13 | 7 |
| β-strand | 373-377 | 5 | 7 |
| β-strand | 382-391 | 10 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-15 | 5 | 9 |
| β-strand | 16-17 | 2 | 10 |
| α-helix | 24-38 | 15 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54-56 | 3 | 11 |
| β-strand | 61-63 | 3 | 11 |
| β-strand | 65-71 | 7 | 9 |
| β-strand | 74-80 | 7 | 9 |
| α-helix | 84-93 | 10 | |
| β-strand | 101-106 | 6 | 10 |
| α-helix | 113-125 | 13 | |
| β-strand | 130-135 | 6 | 10 |
| α-helix | 143-158 | 16 | |
| β-strand | 169-171 | 3 | 10 |
| α-helix | 174-179 | 6 | |
| α-helix | 185-198 | 14 | |
| α-helix | 200-204 | 5 | |
| α-helix | 209-210 | 2 | |
| β-strand | 211-213 | 3 | 12 |
| β-strand | 217-220 | 4 | 12 |
| β-strand | 224-230 | 7 | 12 |
| β-strand | 233 | 1 | 12 |
| β-strand | 235-237 | 3 | 13 |
| β-strand | 241-245 | 5 | 12 |
| β-strand | 251-260 | 10 | 12 |
| β-strand | 263-265 | 3 | 12 |
| β-strand | 267-269 | 3 | 13 |
| β-strand | 273-279 | 7 | 12 |
| α-helix | 283-285 | 3 | |
| β-strand | 288 | 1 | 14 |
| β-strand | 290 | 1 | 14 |
| β-strand | 291-293 | 3 | 12 |
| β-strand | 300-310 | 11 | 15 |
| α-helix | 311-312 | 2 | |
| α-helix | 313-315 | 3 | |
| β-strand | 322 | 1 | 16 |
| β-strand | 329-332 | 4 | 15 |
| β-strand | 335-342 | 8 | 15 |
| α-helix | 343-344 | 2 | |
| β-strand | 350 | 1 | 16 |
| β-strand | 355-367 | 13 | 15 |
| β-strand | 373-378 | 6 | 15 |
| β-strand | 381-391 | 11 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor Tu 1 | A, B | protein | 394 | Escherichia coli | P0CE47 (AlphaFold model) |
| Thiocillin GE2270 analogue NVP-LDK733 | C, D | protein | 12 | Q7M0J8 |
>3U6K_1 Elongation factor Tu 1 (chains A, B) MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
>3U6K_2 Thiocillin GE2270 analogue NVP-LDK733 (chains C, D) SCNCVCGFCCSX
Antibacterial optimization of 4-aminothiazolyl analogues of the natural product GE2270 A: identification of the cycloalkylcarboxylic acids. LaMarche, M.J., Leeds, J.A., Amaral, K. et al. J Med Chem (2011) 54:8099-8109. DOI 10.1021/jm200938f · PubMed
Other PDB entries of the same protein (UniProt P0CE47 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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