› 5a4b

X-ray diffraction
2.01Å resolution

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

Released:
DOI: 10.2210/pdb5a4b/pdb
PDB entry 5a4b coloured by chain, front view.
PDB entry 5a4b coloured by chain, side view.
PDB entry 5a4b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Hypertrophic cardiomyopathy mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation.
Haywood NJ, Wolny M, Rogers B, Trinh CH, Shuping Y, Edwards TA, Peckham M
Biochem J 473 2485-93 (2016)
PMID: 27287556

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152958 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-actinin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 28.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35609 (Residues: 19-266; Coverage: 28%)
Gene name: ACTN2
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 38.39Å b: 46.63Å c: 69.86Å
α: 73.8° β: 80.02° γ: 75.05°
R-values:
R R work R free
0.199 0.198 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

The Role of Z-disc Proteins in Myopathy and Cardiomyopathy.
Wadmore et al. (2021)
6 more

1 mention without citation

Hypertrophic cardiomyopathy mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation.
Haywood et al. (2016)