› 1h67

Solution NMR

NMR Structure of the CH Domain of Calponin

Released:
DOI: 10.2210/pdb1h67/pdb
PDB entry 1h67 coloured by chain, ensemble of 20 models, front view.
PDB entry 1h67 coloured by chain, ensemble of 20 models, side view.
PDB entry 1h67 coloured by chain, ensemble of 20 models, top view.
Source organism: Gallus gallus
Primary publication:
Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin.
Bramham J, Hodgkinson JL, Smith BO, Uhrín D, Barlow PN, Winder SJ
Structure 10 249-58 (2002)
PMID: 11839310

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150887 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calponin-1 Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.27 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26932 (Residues: 28-134; Coverage: 37%)
Gene name: CNN1
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
Chemical shift assignment: 93%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Structural insights into actin-binding, branching and bundling proteins.
Winder SJ. (2003)
19 other articles

5 mentions without citation

Structural Characteristics, Binding Partners and Related Diseases of the Calponin Homology (CH) Domain.
Yin et al. (2020)
4 more