1DG1: Whole, unmodified, ef-tu(elongation factor tu)

Whole, unmodified, ef-tu(elongation factor tu). Determined by X-ray diffraction at 2.5 Å resolution. Released 1 Dec 1999.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Escherichia coli
Chains: 2
Atoms: 6,177
Mol. weight: 87.68 kDa
Ligands: GDP, MG
Released: 1 Dec 1999

Explore 1DG1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DG1 contains 29 α-helices and 54 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.

Chain G: 15 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	1
α-helix	24-39	16
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	113-125	13
β-strand	129-135	7	1
α-helix	143-159	17
α-helix	164-166	3
β-strand	169-171	3	1
α-helix	174-179	6
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	3
β-strand	216-220	5	3
β-strand	224-230	7	3
β-strand	233	1	3
β-strand	235-237	3	4
β-strand	241-245	5	3
β-strand	251-260	10	3
β-strand	263-265	3	3
β-strand	267-269	3	4
β-strand	273-279	7	3
α-helix	283-285	3
β-strand	291-293	3	3
β-strand	300-310	11	5
α-helix	313-315	3
β-strand	322	1	6
β-strand	329-332	4	5
β-strand	335-342	8	5
α-helix	343-344	2
β-strand	350	1	6
β-strand	355-367	13	5
β-strand	373-378	6	5
β-strand	381-391	11	5

Chain H: 14 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	7
α-helix	24-39	16
α-helix	46-50	5
β-strand	54-57	4	8
β-strand	60-63	4	8
β-strand	65-71	7	7
β-strand	74-80	7	7
α-helix	84-93	10
β-strand	100-106	7	7
α-helix	113-125	13
β-strand	130-135	6	7
α-helix	143-159	17
α-helix	164-166	3
β-strand	169-171	3	7
α-helix	174-179	6
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	9
β-strand	216-220	5	9
β-strand	224-230	7	9
β-strand	233	1	9
β-strand	235-237	3	10
β-strand	241-245	5	9
β-strand	251-260	10	9
β-strand	263-265	3	9
β-strand	267-269	3	10
β-strand	273-279	7	9
α-helix	283-285	3
β-strand	291-293	3	9
β-strand	299-310	12	11
α-helix	311-312	2
β-strand	322-323	2	12
β-strand	329-332	4	11
β-strand	335-342	8	11
α-helix	343-344	2
β-strand	349-350	2	12
β-strand	355-368	14	11
β-strand	373-378	6	11
β-strand	381-391	11	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor tu	G, H	protein	394	Escherichia coli	P0CE48 (AlphaFold model)

Sequence of entity 1 (G, H), FASTA

>1DG1_1 ELONGATION FACTOR TU (chains G, H)
MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG
ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI
LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE
GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG
EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK
PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV
VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	2

Primary citation

An alpha to beta conformational switch in EF-Tu. Abel, K., Yoder, M.D., Hilgenfeld, R. et al. Structure (1996) 4:1153-1159. DOI 10.1016/S0969-2126(96)00123-2 · PubMed

Other PDB entries of the same protein (UniProt P0CE48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2BVN 2.3 Å, E. coli EF-Tu:GDPNP in complex with the antibiotic enacyloxin IIa
9T38 2.45 Å, Rhs2-CT endonuclease toxin in complex with cognate immunity protein RhsI2 and EF-Tu
6EZE 2.47 Å, The open conformation of E.coli Elongation Factor Tu in complex with GDPNP.
1EFU 2.5 Å, Elongation factor complex ef-tu/ef-ts from escherichia coli
3MMP 2.5 Å, Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and…
1EFM 2.7 Å, Structure of the GDP domain of ef-tu and location of the amino acids homologous to ras…
8QFS 2.7 Å, Cryo-EM structure of SidH from Legionella pneumophila
5AFI 2.9 Å, 2.9A Structure of E. coli ribosome-EF-TU complex by cs-corrected cryo-EM
5WDT 3.0 Å, 70S ribosome-EF-Tu H84A complex with GppNHp
5WFS 3.0 Å, 70S ribosome-EF-Tu H84A complex with GTP and near-cognate tRNA (Complex C4)
5WE4 3.1 Å, 70S ribosome-EF-Tu wt complex with GppNHp
8G7Q 3.1 Å, Structure of the Escherichia coli 70S ribosome in complex with EF-Tu and…

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