1KTV: Elongation Factor G Dimer Without Nucleotide

Crystal Structure of Elongation Factor G Dimer Without Nucleotide. Determined by X-ray diffraction at 3.8 Å resolution. Released 23 Dec 2003.

Method: X-ray diffraction
Resolution: 3.8 Å
Organism: Thermus thermophilus
Chains: 2
Atoms: 9,914
Mol. weight: 153.95 kDa
Released: 23 Dec 2003

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

Secondary structure: helices and β-sheets

1KTV contains 46 α-helices and 102 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: 24 helices, 52 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	1
α-helix	27-36	10
β-strand	69-74	6	1
β-strand	77-82	6	1
α-helix	96-99	4
β-strand	105-109	5	2
α-helix	116-127	12
β-strand	133-137	5	2
α-helix	146-156	11
β-strand	161-163	3	2
β-strand	167	1	3
β-strand	176-179	4	3
β-strand	184-187	4	3
β-strand	197-199	3	3
α-helix	200-202	3
α-helix	206-223	18
α-helix	225-231	7
α-helix	235-238	4
α-helix	239-251	13
β-strand	256-260	5	2
β-strand	262	1	4
α-helix	263-265	3
β-strand	267	1	4
α-helix	269-279	11
α-helix	281-282	2
α-helix	287-288	2
β-strand	289	1	5
α-helix	290	1
β-strand	292-293	2	6
β-strand	296-298	3	6
β-strand	301	1	5
β-strand	310-318	9	7
β-strand	324-332	9	7
β-strand	334-336	3	8
β-strand	339-342	4	9
α-helix	344-346	3
β-strand	349-352	4	9
β-strand	355-356	2	7
β-strand	366	1	7
β-strand	368-370	3	8
β-strand	376-378	3	7
β-strand	387-390	4	7
β-strand	391	1	9
β-strand	398	1	6
β-strand	413-414	2	10
α-helix	428-431	4
β-strand	441	1	11
β-strand	450	1	11
α-helix	459-463	5
β-strand	480-481	2	10
β-strand	484-486	3	12
β-strand	491-492	2	13
β-strand	495-498	4	14
β-strand	507-511	5	14
β-strand	513-514	2	13
β-strand	515-516	2	15
α-helix	517-518	2
β-strand	519	1	16
β-strand	521	1	16
β-strand	523-527	5	15
α-helix	539-549	11
β-strand	560	1	12
β-strand	563-567	5	15
β-strand	569-571	3	14
β-strand	577	1	14
α-helix	579-584	6
α-helix	586-595	10
β-strand	600-602	3	12
β-strand	603-612	10	17
α-helix	619-626	8
β-strand	633-636	4	17
β-strand	641-646	6	17
α-helix	655-662	8
β-strand	668	1	17
β-strand	671-677	7	17
α-helix	681-687	7

Chain B: 22 helices, 50 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	18
α-helix	25-36	12
β-strand	69-74	6	18
β-strand	77-82	6	18
α-helix	96-99	4
β-strand	105-109	5	19
α-helix	116-128	13
β-strand	133-137	5	19
α-helix	146-156	11
β-strand	161-163	3	19
α-helix	166	1
β-strand	167	1	15
β-strand	176-179	4	15
β-strand	184-187	4	15
β-strand	197-199	3	15
α-helix	206-223	18
α-helix	225-231	7
α-helix	235-237	3
α-helix	239-252	14
β-strand	256-260	5	19
β-strand	262	1	20
α-helix	263-265	3
β-strand	267	1	20
α-helix	269-279	11
α-helix	287-288	2
β-strand	289-293	5	21
β-strand	296-301	6	21
β-strand	310-312	3	22
β-strand	315-318	4	23
β-strand	324-327	4	23
β-strand	330-332	3	22
β-strand	334-336	3	24
β-strand	339-342	4	25
α-helix	344-346	3
β-strand	349-352	4	25
β-strand	354-356	3	23
β-strand	366	1	23
β-strand	368-370	3	24
β-strand	376-378	3	23
β-strand	388-390	3	22
β-strand	391	1	25
β-strand	392	1	26
β-strand	394	1	26
β-strand	398	1	21
β-strand	413-414	2	27
α-helix	428-431	4
α-helix	459-464	6
β-strand	480-481	2	27
β-strand	484-486	3	28
β-strand	491-492	2	29
β-strand	495-496	2	29
β-strand	507	1	30
β-strand	509-516	8	29
α-helix	517-518	2
β-strand	519	1	31
β-strand	521	1	31
β-strand	523-527	5	29
α-helix	539-549	11
β-strand	560	1	28
β-strand	563-571	9	29
β-strand	577	1	30
α-helix	579-584	6
α-helix	586-595	10
β-strand	600-602	3	28
β-strand	603-612	10	32
α-helix	619-626	8
β-strand	630-636	7	32
β-strand	641-648	8	32
α-helix	655-662	8
β-strand	668	1	32
β-strand	671-677	7	32
α-helix	681-687	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor G	A, B	protein	691	Thermus thermophilus	P13551 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1KTV_1 ELONGATION FACTOR G (chains A, B)
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE
RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET
VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV
LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE
ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE
IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA
NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD
QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ
VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP
AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV
ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR
SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ

Primary citation

A New Crystal Form of Thermus thermophilus Elongation Factor G Indicates Crystallographic Limitations Imposed on Molecular Flexibility. Laurberg, M., Kristensen, O., Su, X.D. et al. To be published.

Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2BM0 2.4 Å, Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant T84A
2BV3 2.5 Å, Crystal structure of a mutant elongation factor G trapped with a GTP analogue
2BM1 2.6 Å, Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant G16V
1FNM 2.8 Å, Structure of thermus thermophilus ef-G H573A
2J7K 2.9 Å, Crystal structure of the T84A mutant EF-G:GDPCP complex
4M1K 2.95 Å, Crystal structure of elongation factor G (EFG)
4MYU 3.0 Å, Crystal structure of elongation factor G mutant(EFG)
4MYT 3.5 Å, Crystal structure of elongation factor G (EFG)
1PN6 10.8 Å, Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low…
2BCW 11.2 Å, Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of…
1JQM 18.0 Å, Fitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S…
1JQS 18.0 Å, Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of…

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