Structure of eEF2 in complex with moriniafungin. Determined by X-ray diffraction at 2.9 Å resolution. Released 14 Nov 2006.
Explore 2NPF in 3D Show helices and sheets RCSB PDB PDBe
2NPF contains 80 α-helices and 97 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 | 4 | 1 | 1 |
| α-helix | 6-14 | 9 | |
| α-helix | 16-18 | 3 | |
| β-strand | 19-26 | 8 | 2 |
| α-helix | 32-43 | 12 | |
| β-strand | 44 | 1 | 2 |
| β-strand | 47 | 1 | 1 |
| β-strand | 70 | 1 | 3 |
| β-strand | 74-80 | 7 | 2 |
| α-helix | 85-87 | 3 | |
| β-strand | 97-103 | 7 | 2 |
| α-helix | 112-119 | 8 | |
| β-strand | 124-130 | 7 | 2 |
| β-strand | 134 | 1 | 2 |
| α-helix | 137-148 | 12 | |
| β-strand | 152-158 | 7 | 2 |
| α-helix | 160-161 | 2 | |
| α-helix | 162-166 | 5 | |
| α-helix | 171-192 | 22 | |
| β-strand | 209-213 | 5 | 2 |
| β-strand | 218-220 | 3 | 2 |
| α-helix | 222-228 | 7 | |
| α-helix | 237-243 | 7 | |
| β-strand | 249-251 | 3 | 4 |
| β-strand | 256-258 | 3 | 4 |
| β-strand | 262 | 1 | 5 |
| β-strand | 268 | 1 | 5 |
| β-strand | 271 | 1 | 4 |
| α-helix | 272 | 1 | |
| α-helix | 273-278 | 6 | |
| α-helix | 279-289 | 11 | |
| α-helix | 295-303 | 9 | |
| α-helix | 309-313 | 5 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329 | 1 | 2 |
| α-helix | 330-341 | 12 | |
| α-helix | 343-344 | 2 | |
| α-helix | 345-356 | 12 | |
| β-strand | 357 | 1 | 6 |
| α-helix | 364-371 | 8 | |
| β-strand | 379-387 | 9 | 7 |
| β-strand | 388 | 1 | 3 |
| β-strand | 394-402 | 9 | 7 |
| β-strand | 404-406 | 3 | 8 |
| β-strand | 410-414 | 5 | 7 |
| β-strand | 419 | 1 | 9 |
| β-strand | 422 | 1 | 9 |
| β-strand | 428-430 | 3 | 7 |
| β-strand | 433-438 | 6 | 7 |
| β-strand | 441-445 | 5 | 7 |
| β-strand | 447-449 | 3 | 8 |
| β-strand | 453-457 | 5 | 7 |
| β-strand | 467-470 | 4 | 7 |
| β-strand | 478 | 1 | 6 |
| α-helix | 481-483 | 3 | |
| β-strand | 489-495 | 7 | 10 |
| α-helix | 498-500 | 3 | |
| α-helix | 501-514 | 14 | |
| β-strand | 519-522 | 4 | 10 |
| β-strand | 528-532 | 5 | 10 |
| α-helix | 535-544 | 10 | |
| α-helix | 545-549 | 5 | |
| β-strand | 554-557 | 4 | 10 |
| α-helix | 558-562 | 5 | |
| β-strand | 564-567 | 4 | 11 |
| β-strand | 575-578 | 4 | 12 |
| β-strand | 585-592 | 8 | 12 |
| α-helix | 593-594 | 2 | |
| α-helix | 595-602 | 8 | |
| α-helix | 612-617 | 6 | |
| α-helix | 618-622 | 5 | |
| β-strand | 633-636 | 4 | 12 |
| β-strand | 644-647 | 4 | 12 |
| α-helix | 655-657 | 3 | |
| α-helix | 660-672 | 13 | |
| α-helix | 679-680 | 2 | |
| β-strand | 681 | 1 | 11 |
| β-strand | 684-692 | 9 | 12 |
| α-helix | 697-699 | 3 | |
| α-helix | 702-718 | 17 | |
| β-strand | 722-735 | 14 | 11 |
| α-helix | 740-748 | 9 | |
| β-strand | 753-758 | 6 | 11 |
| β-strand | 766-773 | 8 | 11 |
| α-helix | 774-776 | 3 | |
| α-helix | 780-786 | 7 | |
| β-strand | 793 | 1 | 11 |
| β-strand | 796-804 | 9 | 11 |
| α-helix | 814-826 | 13 | |
| α-helix | 835-837 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 13 |
| α-helix | 6-12 | 7 | |
| α-helix | 16-18 | 3 | |
| β-strand | 19-25 | 7 | 14 |
| α-helix | 32-43 | 12 | |
| β-strand | 44 | 1 | 14 |
| β-strand | 47 | 1 | 13 |
| β-strand | 69 | 1 | 15 |
| β-strand | 70 | 1 | 16 |
| β-strand | 74-80 | 7 | 14 |
| α-helix | 85-87 | 3 | |
| β-strand | 97-103 | 7 | 14 |
| α-helix | 112-119 | 8 | |
| β-strand | 124-130 | 7 | 14 |
| β-strand | 134 | 1 | 14 |
| α-helix | 137-148 | 12 | |
| β-strand | 152-158 | 7 | 14 |
| α-helix | 160-165 | 6 | |
| α-helix | 171-192 | 22 | |
| β-strand | 209-213 | 5 | 14 |
| β-strand | 218-220 | 3 | 14 |
| α-helix | 222-231 | 10 | |
| α-helix | 237-243 | 7 | |
| β-strand | 249-251 | 3 | 17 |
| β-strand | 256-258 | 3 | 17 |
| β-strand | 262 | 1 | 18 |
| β-strand | 268 | 1 | 18 |
| β-strand | 271 | 1 | 17 |
| α-helix | 272-273 | 2 | |
| α-helix | 274-278 | 5 | |
| α-helix | 279-289 | 11 | |
| α-helix | 295-302 | 8 | |
| α-helix | 309-311 | 3 | |
| α-helix | 317-327 | 11 | |
| β-strand | 329 | 1 | 14 |
| α-helix | 330-341 | 12 | |
| α-helix | 343-344 | 2 | |
| α-helix | 345-356 | 12 | |
| β-strand | 357 | 1 | 19 |
| α-helix | 364-371 | 8 | |
| β-strand | 379-387 | 9 | 15 |
| β-strand | 388 | 1 | 16 |
| β-strand | 394-402 | 9 | 15 |
| β-strand | 404-406 | 3 | 20 |
| β-strand | 410-414 | 5 | 15 |
| β-strand | 426-430 | 5 | 15 |
| β-strand | 433-438 | 6 | 15 |
| β-strand | 441-445 | 5 | 15 |
| β-strand | 447-449 | 3 | 20 |
| β-strand | 452-457 | 6 | 15 |
| β-strand | 467-470 | 4 | 15 |
| β-strand | 478 | 1 | 19 |
| β-strand | 489-495 | 7 | 21 |
| α-helix | 498-500 | 3 | |
| α-helix | 501-514 | 14 | |
| β-strand | 519-522 | 4 | 21 |
| β-strand | 528-532 | 5 | 21 |
| α-helix | 535-544 | 10 | |
| α-helix | 545-549 | 5 | |
| β-strand | 554-557 | 4 | 21 |
| α-helix | 558-562 | 5 | |
| β-strand | 564-567 | 4 | 22 |
| β-strand | 575-578 | 4 | 23 |
| β-strand | 585-592 | 8 | 23 |
| α-helix | 593-594 | 2 | |
| α-helix | 595-602 | 8 | |
| α-helix | 612-617 | 6 | |
| α-helix | 618-622 | 5 | |
| α-helix | 630-632 | 3 | |
| β-strand | 633-636 | 4 | 23 |
| β-strand | 644-648 | 5 | 23 |
| α-helix | 660-672 | 13 | |
| α-helix | 679-680 | 2 | |
| β-strand | 681 | 1 | 22 |
| β-strand | 684-692 | 9 | 23 |
| α-helix | 697-699 | 3 | |
| α-helix | 702-718 | 17 | |
| β-strand | 722-735 | 14 | 22 |
| α-helix | 740-749 | 10 | |
| β-strand | 753-758 | 6 | 22 |
| β-strand | 766-773 | 8 | 22 |
| α-helix | 774-776 | 3 | |
| α-helix | 780-786 | 7 | |
| β-strand | 793 | 1 | 22 |
| β-strand | 796-804 | 9 | 22 |
| α-helix | 814-826 | 13 | |
| α-helix | 835-837 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor 2 | A, B | protein | 842 | Saccharomyces cerevisiae | P32324 (AlphaFold model) |
>2NPF_1 Elongation factor 2 (chains A, B) MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTR KDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFAR TVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKM MDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLL EKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGP ADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKV MKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEI CLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLA IENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIK DSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA DPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGF TGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYD KL
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
| MOU | (1S,4R,5R,9S,11S)-2-({[(2S,5R,6R,7R,9S,10R)-2-(7-carboxyheptyl)-6-hydroxy-10-me… | C37 H54 O12 | 2 |
Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2. Soe, R., Mosley, R.T., Justice, M. et al. J Biol Chem (2007) 282:657-666. DOI 10.1074/jbc.M607830200 · 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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