4ezw

X-ray diffraction
1.8Å resolution

Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide NRLLLTG

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, C, D
Molecule details ›
Chains: A, B, C, D
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:
synthetic peptide NRLLLTG Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 7 amino acids
Theoretical weight: 787 Da
Source organism: Escherichia coli K-12
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21212
Unit cell:
a: 157.124Å b: 78.026Å c: 89.482Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.226
Expression systems:
  • Escherichia coli
  • Not provided