Crystal structure of a mutant elongation factor G trapped with a GTP analogue. Determined by X-ray diffraction at 2.5 Å resolution. Released 10 Aug 2005.
Explore 2BV3 in 3D Show helices and sheets RCSB PDB PDBe
2BV3 contains 25 α-helices and 42 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 | 1 | |
| α-helix | 94-100 | 7 | |
| β-strand | 103-109 | 7 | 1 |
| α-helix | 116-126 | 11 | |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 146-155 | 10 | |
| 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 | 225-233 | 9 | |
| α-helix | 235-238 | 4 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 1 |
| β-strand | 262 | 1 | 3 |
| β-strand | 267 | 1 | 3 |
| α-helix | 269-279 | 11 | |
| α-helix | 287-289 | 3 | |
| β-strand | 290-292 | 3 | 4 |
| β-strand | 298-300 | 3 | 4 |
| β-strand | 310-319 | 10 | 5 |
| β-strand | 323-332 | 10 | 5 |
| β-strand | 334-336 | 3 | 6 |
| β-strand | 339-343 | 5 | 5 |
| β-strand | 348-352 | 5 | 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 | 409-410 | 2 | 7 |
| β-strand | 412 | 1 | 8 |
| β-strand | 439-442 | 4 | 8 |
| β-strand | 449-452 | 4 | 8 |
| β-strand | 453 | 1 | 7 |
| α-helix | 456-459 | 4 | |
| β-strand | 480-481 | 2 | 7 |
| β-strand | 484-486 | 3 | 9 |
| β-strand | 491-500 | 10 | 10 |
| β-strand | 505-516 | 12 | 10 |
| β-strand | 523-527 | 5 | 10 |
| α-helix | 536-538 | 3 | |
| α-helix | 539-549 | 11 | |
| β-strand | 560 | 1 | 9 |
| β-strand | 563-571 | 9 | 10 |
| α-helix | 579-596 | 18 | |
| β-strand | 600-613 | 14 | 9 |
| α-helix | 614-616 | 3 | |
| α-helix | 617-625 | 9 | |
| β-strand | 630-637 | 8 | 9 |
| β-strand | 640-648 | 9 | 9 |
| α-helix | 649-651 | 3 | |
| α-helix | 655-661 | 7 | |
| β-strand | 668-678 | 11 | 9 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-686 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | A | protein | 691 | THERMUS THERMOPHILUS | P13551 (AlphaFold model) |
>2BV3_1 ELONGATION FACTOR G (chains A) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEESPTFSVSTHPETGSTIISGMGELSLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Crystal Structure of a Mutant Elongation Factor G Trapped with a GTP Analogue. Hansson, S., Singh, R., Gudkov, A.T. et al. FEBS Lett (2005) 579:4492. DOI 10.1016/J.FEBSLET.2005.07.016 · PubMed
Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2BV3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.