9TBU: E. coli EF-Tu-T62A:GDP AMPylated at T65

E. coli EF-Tu-T62A:GDP AMPylated at T65. Determined by X-ray diffraction at 1.23 Å resolution. Released 12 Aug 2026.

Method: X-ray diffraction
Resolution: 1.23 Å
Organism: Escherichia coli BL21(DE3)
Chains: 1
Atoms: 3,488
Mol. weight: 44.29 kDa
Ligands: MG, AMP, GDP
Released: 12 Aug 2026

Explore 9TBU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9TBU contains 15 α-helices and 28 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 G: 15 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	12-18	7	1
α-helix	25-40	16
α-helix	42-43	2
β-strand	66-71	6	1
β-strand	76-81	6	1
α-helix	85-94	10
β-strand	101-107	7	1
α-helix	114-126	13
β-strand	131-136	6	1
α-helix	138-140	3
α-helix	144-160	17
α-helix	165-167	3
β-strand	170-172	3	1
α-helix	175-179	5
α-helix	183-199	17
α-helix	201-205	5
α-helix	206-208	3
α-helix	210-211	2
β-strand	212-214	3	2
β-strand	217-221	5	3
β-strand	225-231	7	3
β-strand	234	1	2
β-strand	236-238	3	4
β-strand	242-247	6	2
β-strand	249-255	7	2
β-strand	256-261	6	3
β-strand	264-266	3	3
β-strand	268-270	3	4
β-strand	274-279	6	3
α-helix	284-286	3
β-strand	289	1	5
β-strand	291	1	5
β-strand	292-294	3	2
β-strand	301-311	11	6
α-helix	312-313	2
β-strand	323-324	2	7
β-strand	330-333	4	6
β-strand	336-343	8	6
α-helix	344-345	2
β-strand	350-351	2	7
β-strand	356-368	13	6
β-strand	374-379	6	6
β-strand	382-392	11	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor Tu 1	G	protein	396	Escherichia coli BL21(DE3)	P0CE47 (AlphaFold model)

Sequence of entity 1 (G), FASTA

>9TBU_1 Elongation factor Tu 1 (chains G)
GHVSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKA
RGIAINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTRE
HILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKA
LEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK
VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGT
IKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIK
MVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
AMP	Adenosine monophosphate	C10 H14 N5 O7 P	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

Primary citation

The Shewanella oneidensis Fic enzyme SoFic targets the switch-I region of EF-Tu for AMPylation. Runge, S., Pogenberg, V., Baumgart, A. et al. FEBS Lett (2026). DOI 10.1002/1873-3468.70457 · PubMed

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

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…
3U6K 2.45 Å, Ef-tu (escherichia coli) in complex with nvp-ldk733

Browse structure collections

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