Structure analysis

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

X-ray diffraction
2.7Å resolution
Source organism: Homo sapiens
Assembly composition:
Non-polymer only hexamer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: Non-polymer only hexamer
Accessible surface area: 36300 Å2
Buried surface area: 9800 Å2
Dissociation area: 1,400 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 23 kcal/mol
Interface energy (ΔGint): -84 kcal/mol
Symmetry number: 1

Macromolecules

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
Pfam: Ubiquitin-like autophagy protein Apg12
InterPro:
CATH: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

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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
Pfam: Autophagy protein Apg5
InterPro:
CATH:

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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

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