5azg

X-ray diffraction
1.81Å resolution

Crystal structure of LGG-1 complexed with a UNC-51 peptide

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-170809 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein lgg-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 119 amino acids
Theoretical weight: 14.28 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q09490 (Residues: 1-116; Coverage: 94%)
Gene names: C32D5.9, atg-8.1, lgg-1
Sequence domains: Autophagy protein Atg8 ubiquitin like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Serine/threonine-protein kinase unc-51 Chains: C, D
Molecule details ›
Chains: C, D
Length: 10 amino acids
Theoretical weight: 1.25 KDa
Source organism: Caenorhabditis elegans
Expression system: Not provided
UniProt:
  • Canonical: Q23023 (Residues: 352-361; Coverage: 1%)
Gene names: Y60A3A.1, unc-51

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: C2221
Unit cell:
a: 63.684Å b: 80.116Å c: 111.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.212 0.246
Expression systems:
  • Escherichia coli BL21
  • Not provided