Conformation of EF-G during translocation. Determined by electron microscopy. Released 16 Mar 2011.
Explore 3IZP in 3D Show helices and sheets RCSB PDB PDBe
3IZP contains 22 α-helices and 41 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 | 4-10 | 7 | |
| β-strand | 15-19 | 5 | 1 |
| α-helix | 24-37 | 14 | |
| α-helix | 55-60 | 6 | |
| β-strand | 62 | 1 | 1 |
| β-strand | 70-74 | 5 | 2 |
| β-strand | 77-81 | 5 | 2 |
| α-helix | 91-100 | 10 | |
| β-strand | 103-109 | 7 | 1 |
| α-helix | 116-127 | 12 | |
| β-strand | 132-137 | 6 | 1 |
| α-helix | 146-156 | 11 | |
| β-strand | 161-163 | 3 | 1 |
| β-strand | 166-168 | 3 | 3 |
| β-strand | 176-179 | 4 | 3 |
| β-strand | 184-188 | 5 | 3 |
| β-strand | 196-197 | 2 | 3 |
| α-helix | 199 | 1 | |
| β-strand | 200 | 1 | 3 |
| α-helix | 201-202 | 2 | |
| α-helix | 203-221 | 19 | |
| α-helix | 225-233 | 9 | |
| α-helix | 239-251 | 13 | |
| β-strand | 256-260 | 5 | 1 |
| α-helix | 269-279 | 11 | |
| β-strand | 289-292 | 4 | 4 |
| β-strand | 298-301 | 4 | 4 |
| β-strand | 310-318 | 9 | 5 |
| β-strand | 324-332 | 9 | 5 |
| β-strand | 335-336 | 2 | 6 |
| β-strand | 339-343 | 5 | 5 |
| β-strand | 348-358 | 11 | 5 |
| β-strand | 363-366 | 4 | 5 |
| β-strand | 368-369 | 2 | 6 |
| β-strand | 374-379 | 6 | 5 |
| β-strand | 388-390 | 3 | 5 |
| β-strand | 409-413 | 5 | 7 |
| β-strand | 414-415 | 2 | 8 |
| α-helix | 419-434 | 16 | |
| β-strand | 438-439 | 2 | 7 |
| β-strand | 442-443 | 2 | 7 |
| β-strand | 448-453 | 6 | 7 |
| α-helix | 456-465 | 10 | |
| α-helix | 466-470 | 5 | |
| β-strand | 474-475 | 2 | 8 |
| 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 | 563-570 | 8 | 10 |
| β-strand | 577 | 1 | 10 |
| α-helix | 579-596 | 18 | |
| β-strand | 600-612 | 13 | 9 |
| α-helix | 617-626 | 10 | |
| β-strand | 631-637 | 7 | 9 |
| β-strand | 640-648 | 9 | 9 |
| α-helix | 649-651 | 3 | |
| α-helix | 656-662 | 7 | |
| β-strand | 668-678 | 11 | 9 |
| α-helix | 681-684 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor G | E | protein | 688 | Thermus thermophilus | P13551 (AlphaFold model) |
>3IZP_1 Elongation factor G (chains E) MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYAEVDSSEMAFKIAGSMAIKEAVQKGDPV ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR SKTQGRGSFVMFFDHYQEVPKQVQEKLI
Molecular dynamics of EF-G during translocation. Li, W., Trabuco, L.G., Schulten, K. et al. Proteins (2011) 79:1478-1486. DOI 10.1002/prot.22976 · PubMed
Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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