Structure analysis

Electron cryo-microscopy of DNGR-1 in complex with F-actin

Electron Microscopy
7.7Å resolution
Source organisms:
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules


Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 58200 Å2
Buried surface area: 6500 Å2
Dissociation area: 2,100 Å2
Dissociation energy (ΔGdiss): -25 kcal/mol
Dissociation entropy (TΔSdiss): 41 kcal/mol
Interface energy (ΔGint): -44 kcal/mol
Symmetry number: 1


Chain: A
Length: 131 amino acids
Theoretical weight: 14.97 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
  • Canonical: Q8BRU4 (Residues: 108-238; Coverage: 55%)
Gene names: Clec9a, Dngr-1
Pfam: Lectin C-type domain

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Chains: B, C, D
Length: 374 amino acids
Theoretical weight: 41.66 KDa
Source organism: Homo sapiens
  • Canonical: P60709 (Residues: 2-375; Coverage: 100%)
Gene name: ACTB
Pfam: Actin
InterPro: Actin family

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