Structure analysis

Crystal Structure of Activin A Bound to the ECD of ActRIIB

X-ray diffraction
3.1Å resolution
Source organisms:
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 19240.03 Å2
Buried surface area: 3000.03 Å2
Dissociation area: 1,500.01 Å2
Dissociation energy (ΔGdiss): -8.39 kcal/mol
Dissociation entropy (TΔSdiss): 32.26 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140141

Macromolecules

Chains: A, C
Length: 105 amino acids
Theoretical weight: 12.34 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P38445 (Residues: 19-119; Coverage: 20%)
Gene names: Actriib, Acvr2b
Pfam: Activin types I and II receptor domain
InterPro:
CATH: CD59
SCOP: Extracellular domain of cell surface receptors

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Chains: B, D
Length: 116 amino acids
Theoretical weight: 12.99 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P08476 (Residues: 311-426; Coverage: 29%)
Gene name: INHBA
Pfam: Transforming growth factor beta like domain
InterPro:
CATH: Cystine-knot cytokines
SCOP: Transforming growth factor (TGF)-beta

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