› 2n0k

Solution NMR

Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5

Released:
DOI: 10.2210/pdb2n0k/pdb
PDB entry 2n0k coloured by chain, ensemble of 9 models, front view.
PDB entry 2n0k coloured by chain, ensemble of 9 models, side view.
PDB entry 2n0k coloured by chain, ensemble of 9 models, top view.
Source organism: Homo sapiens
Primary publication:
A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis.
Rajagopal P, Tse E, Borst AJ, Delbecq SP, Shi L, Southworth DR, Klevit RE
OpenAccess logo Elife 4 (2015)
PMID: 25962097

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-526563 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-crystallin B chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 89 amino acids
Theoretical weight: 10.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02511 (Residues: 64-152; Coverage: 51%)
Gene names: CRYA2, CRYAB, HSPB5
Sequence domains: Hsp20/alpha crystallin family
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 43%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Protein-Protein Interactions in the Molecular Chaperone Network.
Freilich et al. (2018)
7 more

5 mentions without citation

Mechanisms of Small Heat Shock Proteins.
Janowska et al. (2019)
4 more