› 4b9q

X-ray diffraction
2.4Å resolution

Open conformation of ATP-bound Hsp70 homolog DnaK

Released:
DOI: 10.2210/pdb4b9q/pdb
PDB entry 4b9q coloured by chain, front view.
PDB entry 4b9q coloured by chain, side view.
PDB entry 4b9q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.
Kityk R, Kopp J, Sinning I, Mayer MP
Mol Cell 48 863-74 (2012)
PMID: 23123194

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 605 amino acids
Theoretical weight: 66.27 KDa
Source organism: Escherichia coli
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

2 bound ligands:
Ligand ATP 4 x ATP
Ligand MG 4 x MG
1 modified residue:
Ligand MSE 60 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 202.331Å b: 77.47Å c: 182.96Å
α: 90° β: 101.71° γ: 90°
R-values:
R R work R free
0.199 0.196 0.239
Expression system: Escherichia coli

Quick links

Citations

42 review citations

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

84 mentions without citation

Chaperone machines for protein folding, unfolding and disaggregation.
Saibil H. (2013)
83 more