PDBe 4gdk

X-ray diffraction
2.7Å 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 hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-like protein ATG12 Chains: A, D
Molecule details ›
Chains: A, D
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 Chains: B, E
Molecule details ›
Chains: B, E
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: Autophagy protein Apg5
Structure domains:
Autophagy-related protein 16-1 Chains: C, F
Molecule details ›
Chains: C, F
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: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 43.757Å b: 113.153Å c: 210.685Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.176 0.236
Expression system: Escherichia coli