› 2bpr

Solution NMR

NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, 25 STRUCTURES

Released:
DOI: 10.2210/pdb2bpr/pdb
PDB entry 2bpr coloured by chain, ensemble of 25 models, front view.
PDB entry 2bpr coloured by chain, ensemble of 25 models, side view.
PDB entry 2bpr coloured by chain, ensemble of 25 models, 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-141446 (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

13 review citations

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

2 mentions without citation

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