1TTT: Of elongation factor tu

Phe-tRNA, elongation factoR EF-TU:GDPNP ternary complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 23 Dec 1996.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Thermus aquaticus
Chains: 6
Atoms: 14,573
Mol. weight: 211.11 kDa
Ligands: PHE, GNP, MG
Released: 23 Dec 1996

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

Secondary structure: helices and β-sheets

1TTT contains 46 α-helices and 82 β-strands across 3 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: 17 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	1
β-strand	11-17	7	2
α-helix	24-38	15
α-helix	47-50	4
α-helix	54-55	2
α-helix	56-60	5
β-strand	66-71	6	2
β-strand	76-81	6	2
α-helix	86-88	3
α-helix	89-96	8
β-strand	102-107	6	2
α-helix	114-125	12
β-strand	131-136	6	2
α-helix	138-140	3
α-helix	144-160	17
β-strand	170-172	3	2
α-helix	175-184	10
α-helix	194-209	16
α-helix	211-214	4
α-helix	220-221	2
β-strand	222-224	3	3
β-strand	225-231	7	1
β-strand	235-241	7	1
β-strand	244	1	3
β-strand	246-248	3	4
β-strand	252-256	5	3
β-strand	263-266	4	3
β-strand	267-272	6	1
β-strand	275-276	2	1
β-strand	279-281	3	4
β-strand	285-290	6	1
β-strand	303-305	3	3
β-strand	312-322	11	5
α-helix	323-324	2
α-helix	325-327	3
β-strand	334-335	2	6
β-strand	341-344	4	5
β-strand	347-354	8	5
α-helix	355-356	2
β-strand	361-362	2	6
α-helix	363	1
β-strand	367-379	13	5
β-strand	385-390	6	5
β-strand	393-403	11	5

Chain B: 14 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	7
β-strand	11-17	7	8
α-helix	24-38	15
α-helix	47-49	3
α-helix	54-59	6
β-strand	66-71	6	8
β-strand	76-81	6	8
α-helix	86-88	3
α-helix	89-96	8
β-strand	102-107	6	8
α-helix	114-125	12
β-strand	131-136	6	8
α-helix	144-160	17
β-strand	170-172	3	8
α-helix	175-184	10
α-helix	194-209	16
α-helix	220-221	2
β-strand	222-224	3	9
β-strand	225-231	7	7
β-strand	235-241	7	7
β-strand	244	1	9
β-strand	246-248	3	10
β-strand	252-256	5	9
β-strand	263-266	4	9
β-strand	267-271	5	7
β-strand	275-276	2	7
β-strand	279-281	3	10
β-strand	285-290	6	7
α-helix	295-297	3
β-strand	303-305	3	9
β-strand	312-322	11	11
α-helix	323-324	2
α-helix	325-327	3
β-strand	334	1	12
β-strand	341-344	4	11
β-strand	347-354	8	11
α-helix	355-356	2
β-strand	362	1	12
β-strand	369-379	11	11
β-strand	385-390	6	11
β-strand	393-403	11	11

Chain C: 15 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	13
α-helix	24-38	15
α-helix	54-55	2
α-helix	56-60	5
β-strand	66-71	6	13
β-strand	76-81	6	13
α-helix	86-88	3
α-helix	89-97	9
β-strand	101-107	7	13
α-helix	114-125	12
β-strand	131-136	6	13
α-helix	138-140	3
α-helix	144-160	17
β-strand	170-172	3	13
α-helix	175-184	10
α-helix	194-209	16
α-helix	211-213	3
α-helix	220-221	2
β-strand	222-224	3	14
β-strand	225-231	7	15
β-strand	235-241	7	15
β-strand	244	1	14
β-strand	246-248	3	16
β-strand	252-256	5	14
β-strand	263-266	4	14
β-strand	267-271	5	15
β-strand	276	1	15
β-strand	279-281	3	16
β-strand	285-290	6	15
α-helix	295-297	3
β-strand	300	1	17
β-strand	302	1	17
β-strand	303-305	3	14
β-strand	312-322	11	18
α-helix	323-324	2
β-strand	334	1	19
β-strand	341-344	4	18
β-strand	347-354	8	18
α-helix	355-356	2
β-strand	362	1	19
β-strand	369-379	11	18
β-strand	385-390	6	18
β-strand	393-403	11	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transfer ribonucleic acid (yeast, phe)	D, E, F	RNA	76
Of elongation factor tu (ef-tu)	A, B, C	protein	405	Thermus aquaticus	Q01698 (AlphaFold model)

Sequence of entity 1 (D, E, F), FASTA

>1TTT_1 TRANSFER RIBONUCLEIC ACID (YEAST, PHE) (chains D, E, F)
GCGGAUUUAGCUCAGUUGGGAGAGCGCCAGACUGAAGAUCUGGAGGUCCUGUGUUCGAUC
CACAGAAUUCGCACCA

Sequence of entity 2 (A, B, C), FASTA

>1TTT_2 OF ELONGATION FACTOR TU (EF-TU) (chains A, B, C)
AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDIDKAPEERARG
ITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREHI
LLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQYEFPGDEVPVIRGSALLALE
EMHKNPKTKRGENEWVDKIWELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATG
RIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVTGVVRLPQGVE
MVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE

Ligands and cofactors

ID	Name	Formula	Copies
PHE	Phenylalanine	C9 H11 N O2	3
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	3
MG	Magnesium ion	Mg	6

Primary citation

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Nissen, P., Kjeldgaard, M., Thirup, S. et al. Science (1995) 270:1464-1472. PubMed

Other PDB entries of the same protein (UniProt Q01698 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1EFT 2.5 Å, The crystal structure of elongation factor ef-tu from thermus aquaticus in the GTP…
1B23 2.6 Å, E. coli cysteinyl-tRNA and T. aquaticus elongation factor EF-TU:GTP ternary complex
1TUI 2.7 Å, Intact elongation factor tu in complex with GDP
1OB5 3.1 Å, T. aquaticus elongation factor EF-Tu complexed with the antibiotic enacyloxin IIa, a GTP…

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1TTT is part of these collections:

The ribosome and protein synthesis

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