ADP-AlF4 complex of S. cerevisiae GET3. Determined by X-ray diffraction at 1.99 Å resolution. Released 11 Aug 2009.
Explore 2WOJ in 3D Show helices and sheets RCSB PDB PDBe
2WOJ contains 66 α-helices and 32 β-strands across 4 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 | 10-13 | 4 | |
| β-strand | 20-25 | 6 | 1 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 1 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 1 |
| α-helix | 77 | 1 | |
| β-strand | 83-87 | 5 | 1 |
| α-helix | 90-98 | 9 | |
| α-helix | 125-130 | 6 | |
| α-helix | 136-154 | 19 | |
| β-strand | 162-166 | 5 | 1 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-177 | 8 | |
| α-helix | 179-188 | 10 | |
| α-helix | 213-230 | 18 | |
| β-strand | 236-243 | 8 | 1 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 1 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 1 |
| α-helix | 316-317 | 2 | |
| α-helix | 323-335 | 13 | |
| α-helix | 340-343 | 4 | |
| α-helix | 344-350 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| β-strand | 20-25 | 6 | 2 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 2 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 2 |
| α-helix | 77 | 1 | |
| β-strand | 83-87 | 5 | 2 |
| α-helix | 90-103 | 14 | |
| α-helix | 127-130 | 4 | |
| α-helix | 136-152 | 17 | |
| β-strand | 162-166 | 5 | 2 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-189 | 20 | |
| α-helix | 212-230 | 19 | |
| β-strand | 236-243 | 8 | 2 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 2 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 2 |
| α-helix | 316-317 | 2 | |
| α-helix | 324-335 | 12 | |
| α-helix | 340-343 | 4 | |
| α-helix | 344-348 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| β-strand | 20-25 | 6 | 3 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 3 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 77 | 1 | |
| β-strand | 83-87 | 5 | 3 |
| α-helix | 90-97 | 8 | |
| α-helix | 127-130 | 4 | |
| α-helix | 136-150 | 15 | |
| β-strand | 162-166 | 5 | 3 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-187 | 18 | |
| α-helix | 214-230 | 17 | |
| β-strand | 236-243 | 8 | 3 |
| α-helix | 246-261 | 16 | |
| β-strand | 266-274 | 9 | 3 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 3 |
| α-helix | 316-317 | 2 | |
| α-helix | 323-335 | 13 | |
| α-helix | 340-343 | 4 | |
| α-helix | 346-349 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| β-strand | 20-24 | 5 | 4 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 4 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 77 | 1 | |
| β-strand | 83-87 | 5 | 4 |
| α-helix | 90-103 | 14 | |
| α-helix | 119-122 | 4 | |
| α-helix | 126-130 | 5 | |
| α-helix | 136-150 | 15 | |
| β-strand | 162-166 | 5 | 4 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-188 | 19 | |
| α-helix | 213-230 | 18 | |
| β-strand | 236-243 | 8 | 4 |
| α-helix | 246-261 | 16 | |
| β-strand | 268-274 | 7 | 4 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 4 |
| α-helix | 316-317 | 2 | |
| α-helix | 324-335 | 12 | |
| α-helix | 340-343 | 4 | |
| α-helix | 344-348 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Atpase GET3 | A, B, C, D | protein | 354 | SACCHAROMYCES CEREVISIAE | Q12154 (AlphaFold model) |
>2WOJ_1 ATPASE GET3 (chains A, B, C, D) MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
| MG | Magnesium ion | Mg | 4 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 4 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 4 |
The Structural Basis of Tail-Anchored Membrane Protein Recognition by Get3. Mateja, A., Szlachcic, A., Downing, M.E. et al. Nature (2009) 461:361. DOI 10.1038/NATURE08319 · PubMed
Other PDB entries of the same protein (UniProt Q12154 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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