› 2kho

Solution NMR

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

Released:
DOI: 10.2210/pdb2kho/pdb
PDB entry 2kho coloured by chain, front view.
PDB entry 2kho coloured by chain, side view.
PDB entry 2kho coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.
Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER
Proc Natl Acad Sci U S A 106 8471-6 (2009)
PMID: 19439666

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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

Quick links

Citations

34 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
33 more

171 mentions without citation

The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
Kampinga et al. (2010)
170 more