› 6amn

X-ray diffraction
2.82Å resolution

Crystal Structure of Hsp104 N Domain

Released:
DOI: 10.2210/pdb6amn/pdb
PDB entry 6amn coloured by chain, front view.
PDB entry 6amn coloured by chain, side view.
PDB entry 6amn coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.
Lee J, Sung N, Mercado JM, Hryc CF, Chang C, Lee S, Tsai FTF
Sci Rep 7 11184 (2017)
PMID: 28894176

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152027 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 104 Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 39.08 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P31539 (Residues: 4-352; Coverage: 38%)
Gene names: HSP104, L0948, YLL026W
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P6522
Unit cell:
a: 179.096Å b: 179.096Å c: 69.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.21 0.279
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Differential Interactions of Molecular Chaperones and Yeast Prions.
Barbitoff et al. (2022)
8 other articles

4 mentions without citation

Amyloid management by chaperones: The mystery underlying protein oligomers' dual functions.
Arghavani et al. (2022)
3 more