Structure analysis

Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er)

Electron Microscopy
3.3Å resolution
Assembly composition:
hetero tetramer (preferred)
Entry contents: 4 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 57434.6 Å2
Buried surface area: 6254.46 Å2
Dissociation area: 1,082.23 Å2
Dissociation energy (ΔGdiss): -4.9 kcal/mol
Dissociation entropy (TΔSdiss): 20.59 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-146991

Macromolecules

Chain: A
Length: 792 amino acids
Theoretical weight: 91.36 KDa
Source organism: Gallus gallus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q02440 (Residues: 1-792; Coverage: 43%)
Gene name: MYO5A
Pfam:
InterPro:

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Chain: C
Length: 377 amino acids
Theoretical weight: 42.11 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Pfam: Actin
InterPro:

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Chain: H
Length: 7 amino acids
Theoretical weight: 809 Da
Source organism: Amanita phalloides
Expression system: Not provided

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Chain: B
Length: 151 amino acids
Theoretical weight: 17.09 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P14649 (Residues: 58-208; Coverage: 73%)
Gene names: MLC1SA, MYL6B
InterPro:

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