Elongation factor G in complex with GDP. Determined by X-ray diffraction at 2.4 Å resolution. Released 11 Jul 1996.
Explore 1DAR in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| β-strand | 12-19 | 8 | 1 |
| α-helix | 25-36 | 12 | |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 83-85 | 3 | |
| α-helix | 91-100 | 10 | |
| β-strand | 103-109 | 7 | 1 |
| α-helix | 116-127 | 12 | |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 146-152 | 7 | |
| α-helix | 153-157 | 5 | |
| β-strand | 161-163 | 3 | 1 |
| β-strand | 165-168 | 4 | 2 |
| α-helix | 171-173 | 3 | |
| β-strand | 176-179 | 4 | 2 |
| β-strand | 184-188 | 5 | 2 |
| β-strand | 196-199 | 4 | 2 |
| α-helix | 200-202 | 3 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-220 | 15 | |
| α-helix | 225-233 | 9 | |
| α-helix | 235-238 | 4 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 1 |
| β-strand | 262 | 1 | 3 |
| α-helix | 263-265 | 3 | |
| β-strand | 267 | 1 | 3 |
| α-helix | 269-279 | 11 | |
| α-helix | 281-282 | 2 | |
| β-strand | 289-292 | 4 | 4 |
| β-strand | 298-301 | 4 | 4 |
| β-strand | 310-319 | 10 | 5 |
| β-strand | 323-332 | 10 | 5 |
| β-strand | 334-336 | 3 | 6 |
| β-strand | 340-343 | 4 | 5 |
| β-strand | 348-351 | 4 | 5 |
| β-strand | 354-358 | 5 | 5 |
| β-strand | 363-366 | 4 | 5 |
| β-strand | 368-370 | 3 | 6 |
| β-strand | 374-378 | 5 | 5 |
| β-strand | 388-391 | 4 | 5 |
| β-strand | 398 | 1 | 4 |
| β-strand | 439-441 | 3 | 7 |
| β-strand | 449-453 | 5 | 7 |
| β-strand | 470-472 | 3 | 7 |
| β-strand | 473 | 1 | 8 |
| β-strand | 477 | 1 | 8 |
| β-strand | 481 | 1 | 7 |
| β-strand | 484-486 | 3 | 9 |
| β-strand | 491-499 | 9 | 10 |
| β-strand | 506-516 | 11 | 10 |
| β-strand | 523-527 | 5 | 10 |
| α-helix | 539-549 | 11 | |
| β-strand | 560 | 1 | 9 |
| β-strand | 563-570 | 8 | 10 |
| β-strand | 577 | 1 | 10 |
| α-helix | 579-595 | 17 | |
| β-strand | 600-612 | 13 | 9 |
| α-helix | 619-626 | 8 | |
| β-strand | 631-637 | 7 | 9 |
| β-strand | 640-648 | 9 | 9 |
| α-helix | 655-662 | 8 | |
| β-strand | 668-678 | 11 | 9 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-688 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | Thermus thermophilus | Q5SHN5 (AlphaFold model) |
>1DAR_1 ELONGATION FACTOR G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
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:
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