› 1bpr

Solution NMR

NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1bpr/pdb
PDB entry 1bpr coloured by chain, front view.
PDB entry 1bpr coloured by chain, side view.
PDB entry 1bpr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER
Biochemistry 37 7929-40 (1998)
PMID: 9609686

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 20.94 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6Y8 (Residues: 380-561; Coverage: 29%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Structure domains: Substrate Binding Domain Of DNAk; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS WITH SIMULATED ANNEALING
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

5 mentions without citation

Structural basis of interdomain communication in the Hsc70 chaperone.
Jiang et al. (2005)
4 more