› 1dkx

X-ray diffraction
2Å resolution

THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 SELENOMETHIONYL CRYSTALS

Released:
DOI: 10.2210/pdb1dkx/pdb
PDB entry 1dkx coloured by chain, front view.
PDB entry 1dkx coloured by chain, side view.
PDB entry 1dkx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural analysis of substrate binding by the molecular chaperone DnaK.
Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA
Science 272 1606-14 (1996)
PMID: 8658133

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-141473 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 23.81 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A6Y8 (Residues: 389-607; Coverage: 34%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Structure domains:
SUBSTRATE PEPTIDE (7 RESIDUES) Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 787 Da
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 94.5Å b: 116.6Å c: 37.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.288
Expression system: Not provided

Quick links

Citations

161 review citations

The Hsp70 and Hsp60 chaperone machines.
Bukau et al. (1998)
160 more

49 mentions without citation

Hsp70 chaperones: cellular functions and molecular mechanism.
Mayer et al. (2005)
48 more