1EFC: Intact elongation factor from e.coli

Intact elongation factor from e.coli. Determined by X-ray diffraction at 2.05 Å resolution. Released 18 Mar 1999.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Escherichia coli
Chains: 2
Atoms: 6,444
Mol. weight: 87.41 kDa
Ligands: GDP, MG
Released: 18 Mar 1999

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

Secondary structure: helices and β-sheets

1EFC contains 32 α-helices and 57 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 A: 15 helices, 28 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	84-92	9
β-strand	100-106	7	1
α-helix	113-125	13
β-strand	130-135	6	1
α-helix	143-159	17
α-helix	164-166	3
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
α-helix	209-210	2
β-strand	211-213	3	3
β-strand	216-219	4	4
β-strand	225-230	6	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	291-293	3	3
β-strand	299-310	12	6
α-helix	313-315	3
β-strand	322	1	7
β-strand	329-332	4	6
β-strand	335-342	8	6
α-helix	343-344	2
β-strand	350	1	7
β-strand	355-368	14	6
β-strand	373-378	6	6
β-strand	381-391	11	6

Chain B: 17 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	9-10	2
β-strand	11-15	5	8
β-strand	16-17	2	9
α-helix	24-39	16
α-helix	46-50	5
α-helix	52-53	2
β-strand	54-57	4	10
β-strand	60-63	4	10
β-strand	65-70	6	8
β-strand	75-80	6	8
α-helix	84-92	9
β-strand	101-106	6	9
α-helix	113-125	13
β-strand	130-135	6	9
α-helix	137-139	3
α-helix	143-159	17
α-helix	164-166	3
β-strand	169-171	3	9
α-helix	174-178	5
α-helix	182-198	17
α-helix	205-207	3
α-helix	209-210	2
β-strand	211-213	3	11
β-strand	216-220	5	11
β-strand	224-230	7	11
β-strand	233	1	11
β-strand	235-237	3	12
β-strand	241-246	6	11
β-strand	248-260	13	11
β-strand	263-265	3	11
β-strand	267-269	3	12
β-strand	273-279	7	11
β-strand	281	1	11
α-helix	283-285	3
β-strand	291-293	3	11
β-strand	300-310	11	13
α-helix	311-312	2
α-helix	313-315	3
β-strand	322-323	2	14
β-strand	329-332	4	13
β-strand	335-342	8	13
α-helix	343-344	2
β-strand	349-350	2	14
β-strand	355-367	13	13
β-strand	373-378	6	13
β-strand	381-391	11	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (elongation factor)	A, B	protein	393	Escherichia coli	P0CE47 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1EFC_1 PROTEIN (ELONGATION FACTOR) (chains A, B)
SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGI
TINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHIL
LGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG
DAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGE
EVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKP
HTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVV
TLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS

Ligands and cofactors

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

Primary citation

Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. Song, H., Parsons, M.R., Rowsell, S. et al. J Mol Biol (1999) 285:1245-1256. DOI 10.1006/jmbi.1998.2387 · 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
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…
3U6K 2.45 Å, Ef-tu (escherichia coli) in complex with nvp-ldk733

Browse structure collections

About this viewer

MolViewer shows 1EFC 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.