4gdl

X-ray diffraction
2.88Å resolution

Crystal Structure of Human Atg12~Atg5 Conjugate in Complex with an N-terminal Fragment of Atg16L1

Released:
Source organism: Homo sapiens

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-131765 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-like protein ATG12 Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 10.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94817 (Residues: 52-140; Coverage: 64%)
Gene names: APG12, APG12L, ATG12
Sequence domains: Ubiquitin-like autophagy protein Apg12
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Autophagy protein 5 Chain: B
Molecule details ›
Chain: B
Length: 275 amino acids
Theoretical weight: 32.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H1Y0 (Residues: 1-275; Coverage: 100%)
Gene names: APG5L, ASP, ATG5
Sequence domains:
Structure domains:
Autophagy-related protein 16-1 Chain: C
Molecule details ›
Chain: C
Length: 36 amino acids
Theoretical weight: 4.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q676U5 (Residues: 11-43; Coverage: 5%)
Gene names: APG16L, ATG16L1, UNQ9393/PRO34307

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 136.601Å b: 58.399Å c: 91.802Å
α: 90° β: 130.04° γ: 90°
R-values:
R R work R free
0.219 0.215 0.254
Expression system: Escherichia coli