6prp

Solution NMR

Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

Released:
Source organism: Thermus thermophilus HB8
Primary publication:
Structural basis for client recognition and activity of Hsp40 chaperones.
Science 365 1313-1319 (2019)
PMID: 31604242

Function and Biology Details

Reaction catalysed:
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein DnaJ 2; Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 9.18 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56235 (Residues: 604-615; Coverage: 2%)
  • Canonical: Q56237 (Residues: 190-256; Coverage: 24%)
Gene names: TTHA1489, TTHA1491, dnaJ2, dnaK

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: molecular dynamics
Chemical shifts: BMR30636  
Expression system: Escherichia coli BL21(DE3)