› 4r5g

X-ray diffraction
3.45Å resolution

Crystal structure of the DnaK C-terminus with the inhibitor PET-16

Released:
DOI: 10.2210/pdb4r5g/pdb
PDB entry 4r5g coloured by chain, front view.
PDB entry 4r5g coloured by chain, side view.
PDB entry 4r5g coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket.
Leu JI, Zhang P, Murphy ME, Marmorstein R, George DL
ACS Chem Biol 9 2508-16 (2014)
PMID: 25148104

Function and Biology Details

Biochemical function:
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-141465 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein DnaK Chains: A, B
Molecule details ›
Chains: A, B
Length: 230 amino acids
Theoretical weight: 25.24 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6Y8 (Residues: 389-607; Coverage: 34%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 3JE 1 x 3JE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P43212
Unit cell:
a: 91.778Å b: 91.778Å c: 136.888Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.286 0.284 0.328
Expression system: Escherichia coli

Quick links

Citations

4 review citations

HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.
Wang et al. (2017)
3 more

2 mentions without citation

The remarkable multivalency of the Hsp70 chaperones.
Zuiderweg et al. (2017)
1 more