X-ray diffraction
1.9Å resolution

Crystal structure of the substrate binding domain of E.coli DnaK in complex with the C-terminal part of drosocin (residues 12 to 19)


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero octamer
hetero tetramer
hetero dimer (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: 23.82 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P0A6Y8 (Residues: 389-607; Coverage: 34%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Structure domains:
Drosocin Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 964 Da
Source organism: Drosophila melanogaster
Expression system: Not provided
  • Canonical: P36193 (Residues: 33-40; Coverage: 18%)
Gene names: CG10816, Dro

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: I222
Unit cell:
a: 93.804Å b: 116.433Å c: 36.992Å
α: 90° β: 90° γ: 90°
R R work R free
0.22 0.216 0.29
Expression systems:
  • Escherichia coli
  • Not provided