› 3d2e

X-ray diffraction
2.35Å resolution

Crystal structure of a complex of Sse1p and Hsp70, Selenomethionine-labeled crystals

Released:
DOI: 10.2210/pdb3d2e/pdb
PDB entry 3d2e coloured by chain, front view.
PDB entry 3d2e coloured by chain, side view.
PDB entry 3d2e coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
Polier S, Dragovic Z, Hartl FU, Bracher A
Cell 133 1068-79 (2008)
PMID: 18555782

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143650 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heat shock protein homolog SSE1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 675 amino acids
Theoretical weight: 75.82 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32589 (Residues: 1-502, 525-693; Coverage: 97%)
Gene names: LPG3C, MSI3, SSE1, YPL106C
Sequence domains: Hsp70 protein
Structure domains:
Heat shock 70 kDa protein 1A Chains: B, D
Molecule details ›
Chains: B, D
Length: 382 amino acids
Theoretical weight: 42.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 1-382; Coverage: 60%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand ATP 2 x ATP
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 129.84Å b: 141.649Å c: 150.516Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.21 0.262
Expression system: Escherichia coli

Quick links

Citations

48 review citations

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

8 mentions without citation

Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.
Mayer et al. (2019)
7 more