NMR structure of Atg8-Atg7C30 complex. Determined by solution NMR. Released 16 Nov 2011.
Explore 2LI5 in 3D Show helices and sheets RCSB PDB PDBe
2LI5 contains 6 α-helices and 5 β-strands across 2 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 | 11-24 | 14 | |
| β-strand | 28-31 | 4 | 1 |
| β-strand | 35 | 1 | 2 |
| α-helix | 42-44 | 3 | |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 57-67 | 11 | |
| β-strand | 77-79 | 3 | 2 |
| α-helix | 91-94 | 4 | |
| β-strand | 108-110 | 3 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 616-618 | 3 | |
| α-helix | 627-629 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Autophagy-related protein 8 | A | protein | 117 | Saccharomyces cerevisiae | P38182 (AlphaFold model) |
| Ubiquitin-like modifier-activating enzyme ATG7 | B | protein | 34 | Saccharomyces cerevisiae | P38862 (AlphaFold model) |
>2LI5_1 Autophagy-related protein 8 (chains A) HMKSTFKSEYPFEKRKAESERIADRFPNRIPVICEKAEKSDIPEIDKRKYLVPADLTVGQ FVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQEHKDKDGFLYVTYSGENTFG
>2LI5_2 Ubiquitin-like modifier-activating enzyme ATG7 (chains B) GPHMISGLSVIKQEVERLGNDVFEWEDDESDEIA
Structural basis of Atg8 activation by a homodimeric E1, Atg7. Noda, N.N., Satoo, K., Fujioka, Y. et al. Mol Cell (2011) 44:462-475. DOI 10.1016/j.molcel.2011.08.035 · PubMed
Other PDB entries of the same protein (UniProt P38182 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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