Crystal structure of elongation factor 2. Determined by X-ray diffraction at 2.85 Å resolution. Released 27 Nov 2002.
Explore 1N0V in 3D Show helices and sheets RCSB PDB PDBe
1N0V contains 87 α-helices and 94 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 |
|---|---|---|---|
| α-helix | 6-12 | 7 | |
| α-helix | 16-18 | 3 | |
| β-strand | 19-25 | 7 | 1 |
| α-helix | 28-30 | 3 | |
| α-helix | 32-43 | 12 | |
| β-strand | 44 | 1 | 1 |
| β-strand | 69 | 1 | 2 |
| β-strand | 70 | 1 | 3 |
| β-strand | 74-80 | 7 | 1 |
| α-helix | 83-86 | 4 | |
| β-strand | 97-103 | 7 | 1 |
| α-helix | 109-111 | 3 | |
| α-helix | 112-120 | 9 | |
| β-strand | 124-130 | 7 | 1 |
| β-strand | 134 | 1 | 1 |
| α-helix | 137-148 | 12 | |
| α-helix | 151 | 1 | |
| β-strand | 152-158 | 7 | 1 |
| α-helix | 160-165 | 6 | |
| α-helix | 171-191 | 21 | |
| α-helix | 204-206 | 3 | |
| β-strand | 209-213 | 5 | 1 |
| β-strand | 218-221 | 4 | 1 |
| α-helix | 222-231 | 10 | |
| α-helix | 237-243 | 7 | |
| β-strand | 249-251 | 3 | 4 |
| β-strand | 256-258 | 3 | 4 |
| β-strand | 262-263 | 2 | 5 |
| β-strand | 267-268 | 2 | 5 |
| β-strand | 271 | 1 | 4 |
| α-helix | 272-273 | 2 | |
| α-helix | 274-278 | 5 | |
| α-helix | 279-289 | 11 | |
| α-helix | 295-303 | 9 | |
| α-helix | 309-313 | 5 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329 | 1 | 1 |
| α-helix | 330-341 | 12 | |
| α-helix | 343-344 | 2 | |
| α-helix | 345-356 | 12 | |
| β-strand | 357 | 1 | 6 |
| α-helix | 364-370 | 7 | |
| β-strand | 379-387 | 9 | 2 |
| β-strand | 388 | 1 | 3 |
| β-strand | 394-402 | 9 | 2 |
| β-strand | 404-406 | 3 | 7 |
| β-strand | 410-414 | 5 | 2 |
| β-strand | 426-430 | 5 | 2 |
| β-strand | 433-438 | 6 | 2 |
| β-strand | 441-445 | 5 | 2 |
| β-strand | 447-449 | 3 | 7 |
| β-strand | 453-457 | 5 | 2 |
| α-helix | 460-462 | 3 | |
| β-strand | 467-470 | 4 | 2 |
| β-strand | 478 | 1 | 6 |
| β-strand | 489-495 | 7 | 8 |
| α-helix | 498-500 | 3 | |
| α-helix | 501-514 | 14 | |
| β-strand | 519-522 | 4 | 8 |
| β-strand | 528-532 | 5 | 8 |
| α-helix | 535-544 | 10 | |
| α-helix | 545-549 | 5 | |
| β-strand | 554-556 | 3 | 8 |
| α-helix | 557-559 | 3 | |
| β-strand | 560-561 | 2 | 8 |
| β-strand | 564-567 | 4 | 9 |
| β-strand | 575-578 | 4 | 10 |
| β-strand | 585-592 | 8 | 10 |
| α-helix | 595-602 | 8 | |
| α-helix | 612-623 | 12 | |
| α-helix | 627-631 | 5 | |
| β-strand | 633-636 | 4 | 10 |
| β-strand | 644-648 | 5 | 10 |
| α-helix | 656-659 | 4 | |
| α-helix | 660-672 | 13 | |
| α-helix | 679-680 | 2 | |
| β-strand | 681 | 1 | 9 |
| β-strand | 684-692 | 9 | 10 |
| α-helix | 697-699 | 3 | |
| α-helix | 702-718 | 17 | |
| β-strand | 722-736 | 15 | 9 |
| α-helix | 740-748 | 9 | |
| β-strand | 753-759 | 7 | 9 |
| β-strand | 765-773 | 9 | 9 |
| α-helix | 774-776 | 3 | |
| α-helix | 780-786 | 7 | |
| β-strand | 793 | 1 | 9 |
| β-strand | 796-803 | 8 | 9 |
| α-helix | 814-825 | 12 | |
| α-helix | 832-834 | 3 | |
| α-helix | 835-837 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 11 |
| α-helix | 6-14 | 9 | |
| α-helix | 16-18 | 3 | |
| β-strand | 19-25 | 7 | 12 |
| α-helix | 28-30 | 3 | |
| α-helix | 32-43 | 12 | |
| β-strand | 44 | 1 | 12 |
| β-strand | 46-47 | 2 | 11 |
| β-strand | 69 | 1 | 13 |
| β-strand | 70 | 1 | 14 |
| β-strand | 74-80 | 7 | 12 |
| α-helix | 83-87 | 5 | |
| β-strand | 97-103 | 7 | 12 |
| α-helix | 109-111 | 3 | |
| α-helix | 112-119 | 8 | |
| β-strand | 124-130 | 7 | 12 |
| β-strand | 134 | 1 | 12 |
| α-helix | 137-148 | 12 | |
| β-strand | 152-158 | 7 | 12 |
| α-helix | 161-165 | 5 | |
| α-helix | 171-192 | 22 | |
| α-helix | 204-206 | 3 | |
| β-strand | 209-213 | 5 | 12 |
| β-strand | 218-221 | 4 | 12 |
| α-helix | 222-232 | 11 | |
| α-helix | 237-243 | 7 | |
| β-strand | 249-251 | 3 | 15 |
| β-strand | 256-258 | 3 | 15 |
| β-strand | 271 | 1 | 15 |
| α-helix | 272 | 1 | |
| α-helix | 273-278 | 6 | |
| α-helix | 279-288 | 10 | |
| α-helix | 296-303 | 8 | |
| α-helix | 309-312 | 4 | |
| α-helix | 317-327 | 11 | |
| β-strand | 329 | 1 | 12 |
| α-helix | 330-341 | 12 | |
| α-helix | 343-344 | 2 | |
| α-helix | 345-356 | 12 | |
| β-strand | 357 | 1 | 16 |
| α-helix | 364-371 | 8 | |
| β-strand | 379-387 | 9 | 13 |
| β-strand | 388 | 1 | 14 |
| β-strand | 394-402 | 9 | 13 |
| β-strand | 404-406 | 3 | 17 |
| β-strand | 410-414 | 5 | 13 |
| β-strand | 426-430 | 5 | 13 |
| β-strand | 433-438 | 6 | 13 |
| β-strand | 441-444 | 4 | 13 |
| β-strand | 447-449 | 3 | 17 |
| β-strand | 453-457 | 5 | 13 |
| β-strand | 467-470 | 4 | 13 |
| β-strand | 478 | 1 | 16 |
| β-strand | 489-495 | 7 | 18 |
| α-helix | 498-500 | 3 | |
| α-helix | 501-514 | 14 | |
| β-strand | 519-522 | 4 | 18 |
| β-strand | 528-532 | 5 | 18 |
| α-helix | 535-544 | 10 | |
| α-helix | 545-549 | 5 | |
| β-strand | 554-556 | 3 | 18 |
| β-strand | 560-561 | 2 | 18 |
| β-strand | 564-567 | 4 | 19 |
| β-strand | 575-578 | 4 | 20 |
| β-strand | 585-592 | 8 | 20 |
| α-helix | 593-594 | 2 | |
| α-helix | 595-602 | 8 | |
| α-helix | 612-623 | 12 | |
| α-helix | 627-631 | 5 | |
| β-strand | 633-636 | 4 | 20 |
| β-strand | 644-648 | 5 | 20 |
| α-helix | 656-658 | 3 | |
| α-helix | 660-672 | 13 | |
| α-helix | 679-680 | 2 | |
| β-strand | 681 | 1 | 19 |
| β-strand | 684-692 | 9 | 20 |
| α-helix | 697-699 | 3 | |
| α-helix | 702-718 | 17 | |
| β-strand | 722-736 | 15 | 19 |
| α-helix | 737-739 | 3 | |
| α-helix | 740-748 | 9 | |
| β-strand | 753-759 | 7 | 19 |
| β-strand | 765-773 | 9 | 19 |
| α-helix | 774-776 | 3 | |
| α-helix | 780-788 | 9 | |
| β-strand | 793 | 1 | 19 |
| β-strand | 796-803 | 8 | 19 |
| α-helix | 814-825 | 12 | |
| α-helix | 832-834 | 3 | |
| α-helix | 835-838 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor 2 | C, D | protein | 842 | Saccharomyces cerevisiae | P32324 (AlphaFold model) |
>1N0V_1 Elongation factor 2 (chains C, D) MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTR KDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFAR TVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKM MDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLL EKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGP ADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKV MKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEI CLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLA IENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIK DSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA DPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGF TGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYD KL
Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Joergensen, R., Ortiz, P.A., Carr-Schmid, A. et al. Nat Struct Biol (2003) 10:379-385. DOI 10.1038/nsb923 · PubMed
Other PDB entries of the same protein (UniProt P32324 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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