6AAG: Budding yeast Atg8
Crystal structure of budding yeast Atg8 complexed with the helical AIM of Hfl1. Determined by X-ray diffraction at 2.44 Å resolution. Released 12 Dec 2018.
- Method
- X-ray diffraction
- Resolution
- 2.44 Å
- Organisms
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae (strain YJM789)
- Chains
- 7
- Atoms
- 7,859
- Mol. weight
- 113.34 kDa
- Released
- 12 Dec 2018
Explore 6AAG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6AAG contains 52 α-helices and 62 β-strands across 7 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.
Chain A: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -20--18 | 3 | |
| α-helix | -7--5 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 1 |
| β-strand | 43 | 1 | 2 |
| β-strand | 48-52 | 5 | 1 |
| β-strand | 56 | 1 | 3 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 1 |
| β-strand | 89 | 1 | 4 |
| β-strand | 90 | 1 | 3 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 1 |
Chain B: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -20--18 | 3 | |
| α-helix | -7--5 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 5 |
| β-strand | 43 | 1 | 6 |
| β-strand | 48-52 | 5 | 5 |
| β-strand | 56 | 1 | 7 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 5 |
| β-strand | 80 | 1 | 8 |
| β-strand | 83 | 1 | 8 |
| β-strand | 89 | 1 | 2 |
| β-strand | 90 | 1 | 7 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 5 |
Chain C: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -20--18 | 3 | |
| α-helix | -7--5 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 9 |
| α-helix | 42-43 | 2 | |
| β-strand | 48-52 | 5 | 9 |
| β-strand | 56 | 1 | 10 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 9 |
| β-strand | 80 | 1 | 11 |
| β-strand | 83 | 1 | 11 |
| β-strand | 89 | 1 | 6 |
| β-strand | 90 | 1 | 10 |
| α-helix | 91-98 | 8 | |
| β-strand | 105-110 | 6 | 9 |
Chain D: 7 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -20--18 | 3 | |
| α-helix | -7--5 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 12 |
| β-strand | 48-52 | 5 | 12 |
| β-strand | 56 | 1 | 13 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 12 |
| β-strand | 89 | 1 | 14 |
| β-strand | 90 | 1 | 13 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 12 |
Chain E: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -21--18 | 4 | |
| α-helix | -7--5 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 15 |
| β-strand | 43 | 1 | 14 |
| β-strand | 48-52 | 5 | 15 |
| β-strand | 56 | 1 | 16 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 15 |
| β-strand | 80 | 1 | 17 |
| β-strand | 83 | 1 | 17 |
| β-strand | 89 | 1 | 18 |
| β-strand | 90 | 1 | 16 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 15 |
Chain F: 8 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -22--18 | 5 | |
| α-helix | -7--5 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 19 |
| α-helix | 42 | 1 | |
| β-strand | 43 | 1 | 4 |
| β-strand | 48-52 | 5 | 19 |
| β-strand | 56 | 1 | 20 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 19 |
| β-strand | 80 | 1 | 21 |
| β-strand | 83 | 1 | 21 |
| β-strand | 90 | 1 | 20 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 19 |
Chain G: 9 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | -22--18 | 5 | |
| α-helix | -7--5 | 3 | |
| α-helix | 2-4 | 3 | |
| α-helix | 5-8 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 22 |
| β-strand | 43 | 1 | 18 |
| β-strand | 48-52 | 5 | 22 |
| β-strand | 56 | 1 | 23 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 22 |
| β-strand | 80 | 1 | 24 |
| β-strand | 83 | 1 | 24 |
| α-helix | 85-86 | 2 | |
| β-strand | 90 | 1 | 23 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 22 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Transmembrane protein 184 homolog YKR051W,Autophagy-related protein 8 | A, B, C, D, E, F, G | protein | 140 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae (strain YJM789) | P36142 (AlphaFold model), P38182 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>6AAG_1 Transmembrane protein 184 homolog YKR051W,Autophagy-related protein 8 (chains A, B, C, D, E, F, G)
GPEESWEDDIAGQRTFPEDPNYPVMKSTFKSEYPFEKRKAESERIADRFPNRIPVICEKA
EKSDIPEIDKRKYLVPADLTVGQFVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQ
EHKDKDGFLYVTYSGENTFG
Primary citation
Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein. Liu, X.M., Yamasaki, A., Du, X.M. et al. Elife (2018) 7. DOI 10.7554/eLife.41237 · PubMed
Browse structure collections
About this viewer
MolViewer shows 6AAG directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.