S. cerevisiae Get3 complexed with a cytosolic Get1 fragment. Determined by X-ray diffraction at 3.0 Å resolution. Released 7 Sept 2011.
Explore 3ZS8 in 3D Show helices and sheets RCSB PDB PDBe
3ZS8 contains 33 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 | 61-66 | 6 | |
| β-strand | 75-76 | 2 | 1 |
| α-helix | 77 | 1 | |
| β-strand | 83-87 | 5 | 1 |
| α-helix | 90-95 | 6 | |
| α-helix | 136-153 | 18 | |
| β-strand | 162-166 | 5 | 1 |
| α-helix | 173-175 | 3 | |
| α-helix | 179-194 | 16 | |
| α-helix | 221-230 | 10 | |
| 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 | 324-335 | 12 | |
| α-helix | 340-348 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| β-strand | 20-24 | 5 | 2 |
| α-helix | 31-45 | 15 | |
| β-strand | 51-55 | 5 | 2 |
| α-helix | 61-66 | 6 | |
| β-strand | 75-76 | 2 | 2 |
| α-helix | 77 | 1 | |
| β-strand | 83-87 | 5 | 2 |
| α-helix | 90-97 | 8 | |
| α-helix | 127-132 | 6 | |
| α-helix | 136-156 | 21 | |
| β-strand | 162-166 | 5 | 2 |
| α-helix | 175-177 | 3 | |
| α-helix | 179-189 | 11 | |
| α-helix | 212-230 | 19 | |
| 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 | 1 | |
| α-helix | 324-335 | 12 | |
| α-helix | 340-348 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 539-556 | 18 | |
| α-helix | 565-601 | 37 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 538-556 | 19 | |
| α-helix | 565-594 | 30 | |
| α-helix | 595-597 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Atpase GET3 | A, B | protein | 354 | SACCHAROMYCES CEREVISIAE | Q12154 (AlphaFold model) |
| Golgi to er traffic protein 1 | C, D | protein | 84 | SACCHAROMYCES CEREVISIAE | P53192 (AlphaFold model) |
>3ZS8_1 ATPASE GET3 (chains A, B) MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAH NLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSL LQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLP NTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVC VCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLD QIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE
>3ZS8_2 GOLGI TO ER TRAFFIC PROTEIN 1 (chains C, D) TNKYHEKWISKFAPGNELSKKYLAKVKERHELKEFNNSISAQDNYAKWTKNNRKLDSLDK EINNLKDEIQSENKAFQAHLHKLR
| ID | Name | Formula | Copies |
|---|---|---|---|
| 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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