1DAR: Elongation factor G

Elongation factor G in complex with GDP. Determined by X-ray diffraction at 2.4 Å resolution. Released 11 Jul 1996.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Thermus thermophilus
Chains
1
Atoms
4,893
Mol. weight
77.42 kDa
Ligands
GDP
Released
11 Jul 1996

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

Secondary structure: helices and β-sheets

1DAR contains 23 α-helices and 43 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 A: 23 helices, 43 β-strands

ElementResiduesLengthSheet
α-helix9-113
β-strand12-1981
α-helix25-3612
β-strand69-7461
β-strand77-8261
α-helix83-853
α-helix91-10010
β-strand103-10971
α-helix116-12712
β-strand132-13761
α-helix146-1527
α-helix153-1575
β-strand161-16331
β-strand165-16842
α-helix171-1733
β-strand176-17942
β-strand184-18852
β-strand196-19942
α-helix200-2023
α-helix203-2053
α-helix206-22015
α-helix225-2339
α-helix235-2384
α-helix239-25113
β-strand256-26051
β-strand26213
α-helix263-2653
β-strand26713
α-helix269-27911
α-helix281-2822
β-strand289-29244
β-strand298-30144
β-strand310-319105
β-strand323-332105
β-strand334-33636
β-strand340-34345
β-strand348-35145
β-strand354-35855
β-strand363-36645
β-strand368-37036
β-strand374-37855
β-strand388-39145
β-strand39814
β-strand439-44137
β-strand449-45357
β-strand470-47237
β-strand47318
β-strand47718
β-strand48117
β-strand484-48639
β-strand491-499910
β-strand506-5161110
β-strand523-527510
α-helix539-54911
β-strand56019
β-strand563-570810
β-strand577110
α-helix579-59517
β-strand600-612139
α-helix619-6268
β-strand631-63779
β-strand640-64899
α-helix655-6628
β-strand668-678119
α-helix679-6802
α-helix681-6888

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor GAprotein691Thermus thermophilusQ5SHN5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1DAR_1 ELONGATION FACTOR G (chains A)
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE
RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET
VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV
LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE
ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE
IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA
NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD
QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ
VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP
AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV
ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR
SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Primary citation

The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. al-Karadaghi, S., Aevarsson, A., Garber, M. et al. Structure (1996) 4:555-565. DOI 10.1016/S0969-2126(96)00061-5 · PubMed

Other PDB entries of the same protein (UniProt Q5SHN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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