Crystal structure of LGG-1 complexed with a UNC-51 peptide. Determined by X-ray diffraction at 1.81 Å resolution. Released 30 Dec 2015.
Explore 5AZG in 3D Show helices and sheets RCSB PDB PDBe
5AZG contains 16 α-helices and 17 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 | -1-1 | 3 | |
| α-helix | 4-8 | 5 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 1 |
| α-helix | 36 | 1 | |
| α-helix | 42-44 | 3 | |
| β-strand | 48-52 | 5 | 1 |
| β-strand | 56 | 1 | 2 |
| α-helix | 57-67 | 11 | |
| β-strand | 77-79 | 3 | 1 |
| β-strand | 80 | 1 | 3 |
| β-strand | 83 | 1 | 3 |
| α-helix | 84-86 | 3 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-98 | 8 | |
| α-helix | 104 | 1 | |
| β-strand | 105-110 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-8 | 5 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 4 |
| β-strand | 48-52 | 5 | 4 |
| β-strand | 56 | 1 | 5 |
| α-helix | 57-67 | 11 | |
| β-strand | 77-80 | 4 | 4 |
| β-strand | 83 | 1 | 4 |
| α-helix | 84-86 | 3 | |
| β-strand | 90 | 1 | 5 |
| α-helix | 91-98 | 8 | |
| β-strand | 105-110 | 6 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 358 | 1 | |
| β-strand | 359-360 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 357-358 | 2 | |
| β-strand | 359-360 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein lgg-1 | A, B | protein | 119 | Caenorhabditis elegans | Q09490 (AlphaFold model) |
| Serine/threonine-protein kinase unc-51 | C, D | protein | 10 | Caenorhabditis elegans | Q23023 (AlphaFold model) |
>5AZG_1 Protein lgg-1 (chains A, B) GPHMKWAYKEENNFEKRRAEGDKIRRKYPDRIPVIVEKAPKSKLHDLDKKKYLVPSDLTV GQFYFLIRKRIQLRPEDALFFFVNNVIPQTMTTMGQLYQDHHEEDLFLYIAYSDESVYG
>5AZG_2 Serine/threonine-protein kinase unc-51 (chains C, D) YQESTDFTFL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CD | Cadmium ion | Cd | 14 |
Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy. Wu, F., Watanabe, Y., Guo, X.Y. et al. Mol Cell (2015) 60:914-929. DOI 10.1016/j.molcel.2015.11.019 · PubMed
Other PDB entries of the same protein (UniProt Q09490 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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