S. cerevisiae Get3-ADP-AlF4- complex with a cytosolic Get2 fragment. Determined by X-ray diffraction at 2.1 Å resolution. Released 7 Sept 2011.
Explore 3ZS9 in 3D Show helices and sheets RCSB PDB PDBe
3ZS9 contains 36 α-helices and 16 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 | 20-24 | 5 | 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 | 90-99 | 10 | |
| α-helix | 130-132 | 3 | |
| α-helix | 136-153 | 18 | |
| β-strand | 162-166 | 5 | 1 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-186 | 17 | |
| α-helix | 214-230 | 17 | |
| β-strand | 236-243 | 8 | 1 |
| α-helix | 246-261 | 16 | |
| β-strand | 268-274 | 7 | 1 |
| α-helix | 286-305 | 20 | |
| β-strand | 310-315 | 6 | 1 |
| 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 | 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 | 90-99 | 10 | |
| α-helix | 130-132 | 3 | |
| α-helix | 136-152 | 17 | |
| β-strand | 162-166 | 5 | 2 |
| α-helix | 167-169 | 3 | |
| α-helix | 170-196 | 27 | |
| α-helix | 213-230 | 18 | |
| β-strand | 236-243 | 8 | 2 |
| α-helix | 246-261 | 16 | |
| β-strand | 268-274 | 7 | 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 | 506-521 | 16 | |
| α-helix | 525-533 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 506-520 | 15 | |
| α-helix | 525-536 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Atpase GET3 | A, B | protein | 354 | SACCHAROMYCES CEREVISIAE | Q12154 (AlphaFold model) |
| Golgi to er traffic protein 2 | C, D | protein | 38 | SACCHAROMYCES CEREVISIAE | P40056 (AlphaFold model) |
>3ZS9_1 ATPASE GET3 (chains A, B) MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE
>3ZS9_2 GOLGI TO ER TRAFFIC PROTEIN 2 (chains C, D) MSELTEAEKRRLLRERRQKKFSNGGASSRLNKITGQAS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 2 |
| MG | Magnesium ion | Mg | 2 |
| ZN | Zinc ion | Zn | 1 |
The Mechanism of Membrane-Associated Steps in Tail-Anchored Protein Insertion. Mariappan, M., Mateja, A., Dobosz, M. et al. Nature (2011) 477:61. DOI 10.1038/NATURE10362 · 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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