Structure analysis

Crystal structure of the formin homology 2 domain of FMNL3 bound to actin

X-ray diffraction
3.4Å resolution
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: 63051.18 Å2
Buried surface area: 18316.35 Å2
Dissociation area: 3,487.36 Å2
Dissociation energy (ΔGdiss): 0.66 kcal/mol
Dissociation entropy (TΔSdiss): 29.71 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-159318
Assembly 2
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Multimeric state: hetero tetramer
Accessible surface area: 63071.11 Å2
Buried surface area: 18369.96 Å2
Dissociation area: 3,538.92 Å2
Dissociation energy (ΔGdiss): 1.54 kcal/mol
Dissociation entropy (TΔSdiss): 29.73 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-159318

Macromolecules

Chains: D, F, G, H
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Pfam: Actin
InterPro:
CATH:

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Chains: A, B, C, E
Length: 402 amino acids
Theoretical weight: 46.01 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6ZPF4 (Residues: 555-954; Coverage: 39%)
Gene names: Fmnl3, Frl2, Kiaa2014
Pfam: Formin Homology 2 Domain
InterPro:
CATH: Formin, FH2 domain

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