Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae. Determined by X-ray diffraction at 2.6 Å resolution. Released 14 Sept 2004.
Explore 1U2R in 3D Show helices and sheets RCSB PDB PDBe
1U2R contains 44 α-helices and 47 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 |
|---|---|---|---|
| β-strand | 4 | 1 | 1 |
| α-helix | 6-12 | 7 | |
| 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 | 83-88 | 6 | |
| β-strand | 97-103 | 7 | 2 |
| α-helix | 113-120 | 8 | |
| β-strand | 124-130 | 7 | 2 |
| β-strand | 134 | 1 | 2 |
| α-helix | 137-147 | 11 | |
| α-helix | 151 | 1 | |
| β-strand | 152-158 | 7 | 2 |
| α-helix | 160-165 | 6 | |
| α-helix | 171-192 | 22 | |
| α-helix | 195-197 | 3 | |
| α-helix | 204-206 | 3 | |
| β-strand | 209-213 | 5 | 2 |
| β-strand | 218-221 | 4 | 2 |
| α-helix | 222-233 | 12 | |
| 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 | 272-273 | 2 | |
| α-helix | 274-278 | 5 | |
| α-helix | 279-289 | 11 | |
| α-helix | 296-302 | 7 | |
| 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 | 364-370 | 7 | |
| 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 | 426-430 | 5 | 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 |
| α-helix | 476-477 | 2 | |
| β-strand | 478 | 1 | 6 |
| α-helix | 480-482 | 3 | |
| β-strand | 489-495 | 7 | 9 |
| α-helix | 498-500 | 3 | |
| α-helix | 501-514 | 14 | |
| β-strand | 519-522 | 4 | 9 |
| β-strand | 528-532 | 5 | 9 |
| α-helix | 535-544 | 10 | |
| α-helix | 545-549 | 5 | |
| β-strand | 554-557 | 4 | 9 |
| α-helix | 558-562 | 5 | |
| β-strand | 564-567 | 4 | 10 |
| β-strand | 575-578 | 4 | 11 |
| β-strand | 585-592 | 8 | 11 |
| α-helix | 593-594 | 2 | |
| α-helix | 595-603 | 9 | |
| α-helix | 612-621 | 10 | |
| α-helix | 627-631 | 5 | |
| β-strand | 633-636 | 4 | 11 |
| β-strand | 644-648 | 5 | 11 |
| α-helix | 656-672 | 17 | |
| α-helix | 679 | 1 | |
| β-strand | 680-681 | 2 | 10 |
| β-strand | 684-692 | 9 | 11 |
| α-helix | 697-699 | 3 | |
| α-helix | 702-718 | 17 | |
| β-strand | 722-735 | 14 | 10 |
| α-helix | 737-749 | 13 | |
| β-strand | 753-758 | 6 | 10 |
| β-strand | 766-773 | 8 | 10 |
| α-helix | 774-776 | 3 | |
| α-helix | 780-787 | 8 | |
| β-strand | 793 | 1 | 10 |
| β-strand | 796-803 | 8 | 10 |
| α-helix | 814-825 | 12 | |
| α-helix | 832-834 | 3 | |
| α-helix | 835-838 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongation factor 2 | A | protein | 842 | Saccharomyces cerevisiae | P32324 (AlphaFold model) |
>1U2R_1 Elongation factor 2 (chains A) MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTR KDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFAR TVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKM MDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLL EKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGP ADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKV MKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEI CLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLA IENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIK DSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA DPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGF TGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYD KL
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| APR | Adenosine-5-diphosphoribose | C15 H23 N5 O14 P2 | 1 |
| SO1 | [1R-(1.ALPHA.,3A.BETA.,4.BETA.,4A.BETA.,7.BETA.,7A.ALPHA.,8A.BETA.)]8A-[(6-deox… | C27 H42 O8 | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae. Jorgensen, R., Yates, S.P., Teal, D.J. et al. J Biol Chem (2004) 279:45919-45925. DOI 10.1074/jbc.M406218200 · 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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