Translational elongation factor G complexed with GDP. Determined by X-ray diffraction at 2.6 Å resolution. Released 30 Sept 1999.
Explore 2EFG in 3D Show helices and sheets RCSB PDB PDBe
2EFG contains 28 α-helices and 42 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-19 | 8 | 1 |
| α-helix | 25-37 | 13 | |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 91-100 | 10 | |
| β-strand | 103-109 | 7 | 1 |
| β-strand | 113 | 1 | 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 | 206-221 | 16 | |
| α-helix | 225-232 | 8 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 1 |
| β-strand | 262 | 1 | 3 |
| β-strand | 267 | 1 | 3 |
| α-helix | 269-278 | 10 | |
| α-helix | 287-288 | 2 | |
| β-strand | 289-291 | 3 | 4 |
| β-strand | 292 | 1 | 5 |
| β-strand | 299-301 | 3 | 4 |
| β-strand | 310-317 | 8 | 1 |
| β-strand | 325-332 | 8 | 1 |
| β-strand | 335-336 | 2 | 6 |
| β-strand | 339-342 | 4 | 1 |
| β-strand | 349-352 | 4 | 1 |
| β-strand | 354-359 | 6 | 1 |
| β-strand | 362-366 | 5 | 1 |
| β-strand | 368-369 | 2 | 6 |
| β-strand | 374-378 | 5 | 1 |
| β-strand | 388-391 | 4 | 1 |
| β-strand | 398 | 1 | 5 |
| β-strand | 484-486 | 3 | 7 |
| β-strand | 491-498 | 8 | 8 |
| β-strand | 507-516 | 10 | 8 |
| β-strand | 523-527 | 5 | 8 |
| α-helix | 536-538 | 3 | |
| α-helix | 539-549 | 11 | |
| β-strand | 560 | 1 | 7 |
| β-strand | 563-571 | 9 | 8 |
| α-helix | 579-595 | 17 | |
| β-strand | 600-613 | 14 | 7 |
| α-helix | 617-623 | 7 | |
| α-helix | 624-627 | 4 | |
| β-strand | 631-633 | 3 | 9 |
| β-strand | 640-643 | 4 | 7 |
| β-strand | 644-645 | 2 | 9 |
| β-strand | 646-648 | 3 | 7 |
| α-helix | 649-652 | 4 | |
| α-helix | 656-659 | 4 | |
| α-helix | 660-662 | 3 | |
| β-strand | 668-678 | 11 | 7 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-687 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 706-710 | 5 | |
| α-helix | 711-713 | 3 | |
| β-strand | 723 | 1 | 10 |
| β-strand | 730 | 1 | 10 |
| α-helix | 763-766 | 4 | |
| α-helix | 767-770 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (elongation factor G) | A | protein | 691 | Thermus thermophilus | Q5SHN5 (AlphaFold model) |
| Protein (elongation factor G domain 3) | B | protein | 88 | Thermus thermophilus |
>2EFG_1 PROTEIN (ELONGATION FACTOR G) (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDNAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
>2EFG_2 PROTEIN (ELONGATION FACTOR G DOMAIN 3) (chains B) XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXXXXXXXXXX
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. Czworkowski, J., Wang, J., Steitz, T.A. et al. EMBO J (1994) 13:3661-3668. PubMed
Other PDB entries of the same protein (UniProt Q5SHN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
2EFG is part of these collections:
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