Structure of the GDP domain of ef-tu and location of the amino acids homologous to ras oncogene proteins. Determined by X-ray diffraction at 2.7 Å resolution. Released 16 Jul 1987.
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| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor tu | A | protein | 379 | Escherichia coli | P0CE48 (AlphaFold model) |
>1EFM_1 ELONGATION FACTOR TU (chains A) SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARGITINTSHVEYDTPTR HYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFL NKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGF LDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKST CTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKD EGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRF AIREGGRTVGAGVVAKVLS
Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Jurnak, F. Science (1985) 230:32-36. PubMed
Other PDB entries of the same protein (UniProt P0CE48 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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