1EFU: Elongation factor tu

Elongation factor complex ef-tu/ef-ts from escherichia coli. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 Jan 1997.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Escherichia coli
Chains: 4
Atoms: 11,023
Mol. weight: 145.13 kDa
Released: 11 Jan 1997

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

Secondary structure: helices and β-sheets

1EFU contains 51 α-helices and 72 β-strands across 4 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 A: 13 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	11-18	8	1
α-helix	24-39	16
β-strand	67-70	4	1
β-strand	75-80	6	1
α-helix	84-92	9
β-strand	100-106	7	1
α-helix	115-124	10
β-strand	130-135	6	1
α-helix	137-139	3
α-helix	143-158	16
β-strand	169-171	3	1
α-helix	174-178	5
α-helix	182-198	17
α-helix	200-204	5
α-helix	205-207	3
β-strand	211-213	3	2
β-strand	216-218	3	3
β-strand	225-230	6	3
β-strand	233	1	2
β-strand	235-237	3	4
β-strand	241-246	6	2
β-strand	248-254	7	2
β-strand	255-260	6	3
β-strand	263-265	3	3
β-strand	267-269	3	4
β-strand	273-278	6	3
α-helix	283-285	3
β-strand	291-293	3	2
β-strand	300-310	11	5
α-helix	311-312	2
α-helix	313-315	3
β-strand	322-323	2	6
β-strand	329-332	4	5
β-strand	335-342	8	5
α-helix	343-344	2
β-strand	349-350	2	6
β-strand	355-367	13	5
β-strand	373-378	6	5
β-strand	381-391	11	5

Chain B: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	19-28	10
α-helix	33-51	19
β-strand	58-66	9	7
β-strand	69-77	9	7
α-helix	80-83	4
α-helix	86-101	16
α-helix	107-125	19
β-strand	130-138	9	7
β-strand	141-147	7	8
β-strand	151-158	8	8
α-helix	162-175	14
β-strand	179	1	9
α-helix	182-184	3
α-helix	187-203	17
α-helix	208-226	19
β-strand	227	1	9
β-strand	232-233	2	10
β-strand	236-240	5	10
α-helix	241-246	6
β-strand	251-259	9	8
α-helix	271-278	8

Chain C: 14 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	11-18	8	11
α-helix	24-39	16
β-strand	67-70	4	11
β-strand	75-80	6	11
α-helix	84-92	9
β-strand	100-106	7	11
α-helix	115-124	10
β-strand	130-135	6	11
α-helix	137-139	3
α-helix	143-159	17
α-helix	164-166	3
β-strand	169-171	3	11
α-helix	174-178	5
α-helix	182-198	17
α-helix	200-204	5
α-helix	209-210	2
β-strand	211-213	3	12
β-strand	217-219	3	13
β-strand	225-230	6	13
β-strand	233	1	12
β-strand	235-237	3	14
β-strand	241-246	6	12
β-strand	248-254	7	12
β-strand	258-260	3	13
β-strand	263-265	3	13
β-strand	267-269	3	14
β-strand	273-277	5	13
α-helix	283-285	3
β-strand	291-293	3	12
β-strand	300-310	11	15
α-helix	311-312	2
α-helix	313-315	3
β-strand	322-323	2	16
β-strand	329-332	4	15
β-strand	335-342	8	15
α-helix	343-344	2
β-strand	349-350	2	16
β-strand	355-367	13	15
β-strand	373-378	6	15
β-strand	381-391	11	15

Chain D: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
α-helix	19-29	11
α-helix	33-51	19
β-strand	58-66	9	17
β-strand	69-77	9	17
α-helix	80-84	5
α-helix	86-101	16
α-helix	107-125	19
β-strand	130-138	9	17
β-strand	141-147	7	18
β-strand	151-158	8	18
α-helix	162-175	14
β-strand	179	1	19
α-helix	182-184	3
α-helix	187-203	17
α-helix	208-226	19
β-strand	227	1	19
β-strand	232-233	2	20
β-strand	236-240	5	20
α-helix	241-246	6
β-strand	251-259	9	18
α-helix	271-278	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor tu	A, C	protein	385	Escherichia coli	P0CE48 (AlphaFold model)
Elongation factor ts	B, D	protein	282	Escherichia coli	P0A6P1 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1EFU_1 ELONGATION FACTOR TU (chains A, C)
KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVE
YDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVP
YIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKI
LELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIK
ETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEV
YILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAM
DDGLRFAIREGGRTVGAGVVAKVLS

Sequence of entity 2 (B, D), FASTA

>1EFU_2 ELONGATION FACTOR TS (chains B, D)
AEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRKSGAIKAAKKAGNVAADGV
IKTKIDGNYGIILEVNCQTDFVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVA
LVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADEELVKHIAMHVAASKPEFI
KPEDVSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKT
VGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS

Primary citation

The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Kawashima, T., Berthet-Colominas, C., Wulff, M. et al. Nature (1996) 379:511-518. DOI 10.1038/379511a0 · 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.
1DG1 2.5 Å, Whole, unmodified, ef-tu(elongation factor tu).
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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