› 1q5l

Solution NMR

NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG

Released:
DOI: 10.2210/pdb1q5l/pdb
PDB entry 1q5l coloured by chain, ensemble of 15 models, front view.
PDB entry 1q5l coloured by chain, ensemble of 15 models, side view.
PDB entry 1q5l coloured by chain, ensemble of 15 models, top view.
Source organisms:
Primary publication:
The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.
Stevens SY, Cai S, Pellecchia M, Zuiderweg ER
Protein Sci 12 2588-96 (2003)
PMID: 14573869

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141454 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
Length: 135 amino acids
Theoretical weight: 14.47 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6Y8 (Residues: 393-507; Coverage: 18%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Structure domains: Substrate Binding Domain Of DNAk; Chain A, domain 1
peptide NRLLLTG Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 787 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

11 review citations

Hsp70 chaperone dynamics and molecular mechanism.
Mayer MP. (2013)
10 more

4 mentions without citation

A History of Molecular Chaperone Structures in the Protein Data Bank.
Bascos et al. (2019)
3 more