1ETU: Elongation factor tu

Structural details of the binding of guanosine diphosphate to elongation factor tu from E. Coli as studied by X-ray crystallography. Determined by X-ray diffraction at 2.9 Å resolution. Released 16 Jul 1988.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Escherichia coli
Chains: 1
Atoms: 1,395
Mol. weight: 43.68 kDa
Ligands: MG, GDP
Released: 16 Jul 1988

Explore 1ETU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ETU contains 6 α-helices and 6 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.

Chain A: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	1
α-helix	24-39	16
β-strand	65-70	6	1
β-strand	75-80	6	1
α-helix	84-92	9
β-strand	100-105	6	1
α-helix	113-125	13
β-strand	129-135	7	1
α-helix	143-160	18
β-strand	169-172	4	1
α-helix	174-179	6
α-helix	183-198	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor tu	A	protein	393	Escherichia coli	P0CE47 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ETU_1 ELONGATION FACTOR TU (chains A)
SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGI
TINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHIL
LGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG
DAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGE
EVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKP
HTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVV
TLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

Primary citation

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. la Cour, T.F., Nyborg, J., Thirup, S. et al. EMBO J (1985) 4:2385-2388. PubMed

Other PDB entries of the same protein (UniProt P0CE47 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9TBU 1.23 Å, E. coli EF-Tu-T62A:GDP AMPylated at T65
4PC3 1.83 Å, Elongation factor Tu:Ts complex with partially bound GDP
5JBQ 2.01 Å, Ef-tu (escherichia coli) in complex with thiomuracin analog
1EFC 2.05 Å, Intact elongation factor from e.coli
2HCJ 2.12 Å, Trypsin-modified Elongation Factor Tu in complex with tetracycline
3U6B 2.12 Å, Ef-tu (escherichia coli) in complex with nvp-ldi028
4P3Y 2.15 Å, Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu
5MI8 2.18 Å, Structure of the phosphomimetic mutant of EF-Tu T383E
8FR3 2.23 Å, E. coli EF-Tu in complex with KKL-55
4G5G 2.3 Å, ef-tu (Escherichia coli) complexed with nvp-ldu796
1D8T 2.35 Å, Crystal structure of elongation factor, tu (ef-tu-mggdp) complexed with GE2270A, a…
5I4Q 2.35 Å, Contact-dependent inhibition system from Escherichia coli NC101 - ternary…

Browse structure collections

About this viewer

MolViewer shows 1ETU 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.