4e81

X-ray diffraction
1.9Å resolution

Crystal structure of the substrate binding domain of E.coli DnaK in complex with a short apidaecin peptide

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein DnaK Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 23.82 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
Structure domains:
Apidaecin-1A Chains: C, D
Molecule details ›
Chains: C, D
Length: 10 amino acids
Theoretical weight: 1.21 KDa
Source organism: Apis mellifera
Expression system: Not provided
UniProt:
  • Canonical: Q06602 (Residues: 268-279; Coverage: 4%)
Gene name: APID73

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21212
Unit cell:
a: 144.777Å b: 60.202Å c: 67.453Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.259
Expression systems:
  • Escherichia coli
  • Not provided