› 1nlt

X-ray diffraction
2.7Å resolution

The crystal structure of Hsp40 Ydj1

Released:
DOI: 10.2210/pdb1nlt/pdb
PDB entry 1nlt coloured by chain, front view.
PDB entry 1nlt coloured by chain, side view.
PDB entry 1nlt coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate.
Li J, Qian X, Sha B
Structure 11 1475-83 (2003)
PMID: 14656432

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150486 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitochondrial protein import protein MAS5 Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 27.39 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25491 (Residues: 103-350; Coverage: 61%)
Gene names: MAS5, N2418, YDJ1, YNL064C, YNL2418C
Sequence domains:
Structure domains:
Seven residue peptide Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 867 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2, APS BEAMLINE 14-BM-D
Spacegroup: P3221
Unit cell:
a: 55.025Å b: 55.025Å c: 161.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.269 0.269 0.296
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

24 review citations

The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
Kampinga et al. (2010)
23 more

33 mentions without citation

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