2LI5: Atg8-Atg7C30 complex

NMR structure of Atg8-Atg7C30 complex. Determined by solution NMR. Released 16 Nov 2011.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
1,226
Mol. weight
17.45 kDa
Released
16 Nov 2011

Explore 2LI5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 4 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix11-2414
β-strand28-3141
β-strand3512
α-helix42-443
β-strand49-5241
α-helix57-6711
β-strand77-7932
α-helix91-944
β-strand108-11032
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix616-6183
α-helix627-6293

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Autophagy-related protein 8Aprotein117Saccharomyces cerevisiaeP38182 (AlphaFold model)
Ubiquitin-like modifier-activating enzyme ATG7Bprotein34Saccharomyces cerevisiaeP38862 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LI5_1 Autophagy-related protein 8 (chains A)
HMKSTFKSEYPFEKRKAESERIADRFPNRIPVICEKAEKSDIPEIDKRKYLVPADLTVGQ
FVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQEHKDKDGFLYVTYSGENTFG
Sequence of entity 2 (B), FASTA
>2LI5_2 Ubiquitin-like modifier-activating enzyme ATG7 (chains B)
GPHMISGLSVIKQEVERLGNDVFEWEDDESDEIA

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 2LI5 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.