Solution NMR

Solution Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Heat shock protein beta-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 98 amino acids
Theoretical weight: 10.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P04792 (Residues: 80-176; Coverage: 47%)
Gene names: HSP27, HSP28, HSPB1
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 22%
Refinement method: molecular dynamics
Chemical shifts: BMR25645  
Expression system: Escherichia coli