› 6pri

Solution NMR

Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

Released:
DOI: 10.2210/pdb6pri/pdb
PDB entry 6pri coloured by chain, ensemble of 20 models, front view.
PDB entry 6pri coloured by chain, ensemble of 20 models, side view.
PDB entry 6pri coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Structural basis for client recognition and activity of Hsp40 chaperones.
Jiang Y, Rossi P, Kalodimos CG
Science 365 1313-1319 (2019)
PMID: 31604242

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkaline phosphatase; Chaperone protein DnaJ 2 Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.05 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00634 (Residues: 437-447; Coverage: 2%)
  • Canonical: Q56237 (Residues: 192-256; Coverage: 23%)
Gene names: JW0374, TTHA1489, b0383, dnaJ2, phoA
Sequence domains: DnaJ C terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

HSP70 Multi-Functionality in Cancer.
Albakova et al. (2020)
16 more

1 mention without citation

Structural basis for client recognition and activity of Hsp40 chaperones.
Jiang et al. (2019)