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Mutations in the Calponin homology domain of Alpha-Actinin-2 affect Actin binding and incorporation in muscle.

X-ray diffraction
2Å resolution
PDB entry 5a36 coloured by chain, front view.
PDB entry 5a36 coloured by chain, side view.
PDB entry 5a36 coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Alpha-actinin-2
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Multimeric state: monomeric
Accessible surface area: 12618.07 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-152958
Assembly 2
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Assembly Name: Alpha-actinin-2
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Multimeric state: monomeric
Accessible surface area: 11011.52 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-152958

Macromolecules

Alpha-actinin-2
Chains: A, B
Length: 250 amino acids
Theoretical weight: 28.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35609 (Residues: 19-266; Coverage: 28%)
Gene name: ACTN2
Pfam: Calponin homology (CH) domain
InterPro:
CATH: Calponin-like domain
Alpha-actinin-2 in PDB entry 5a36, assembly 1, front view.
Alpha-actinin-2 in PDB entry 5a36, assembly 1, side view.
Alpha-actinin-2 in PDB entry 5a36, assembly 1, top view.
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