› 4r5i

X-ray diffraction
1.97Å resolution

Crystal structure of the DnaK C-terminus with the substrate peptide NRLLLTG

Released:
DOI: 10.2210/pdb4r5i/pdb
PDB entry 4r5i coloured by chain, front view.
PDB entry 4r5i coloured by chain, side view.
PDB entry 4r5i coloured by chain, top view.
Source organisms:
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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141461 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
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:
HSP70/DnaK Substrate Peptide: NRLLLTG Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 787 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I222
Unit cell:
a: 48.243Å b: 57.911Å c: 180.076Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.174 0.218
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

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

1 mention without citation

Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.
Chen et al. (2022)