Solution NMR

NMR-RDC / XRAY structure of E. coli HSP70 (DNAK) chaperone (1-605) complexed with ADP and substrate


Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
Length: 605 amino acids
Theoretical weight: 65.65 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P0A6Y8 (Residues: 1-605; Coverage: 95%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RDC OPTIMIZATION
Expression system: Escherichia coli