› 3d2f

X-ray diffraction
2.3Å resolution

Crystal structure of a complex of Sse1p and Hsp70

Released:
DOI: 10.2210/pdb3d2f/pdb
PDB entry 3d2f coloured by chain, front view.
PDB entry 3d2f coloured by chain, side view.
PDB entry 3d2f 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-534137 (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: 75.31 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: 42.08 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

4 bound ligands:
Ligand MG 6 x MG
Ligand K 2 x K
Ligand ATP 2 x ATP
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 129.5Å b: 141.902Å c: 151.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.244
Expression system: Escherichia coli

Quick links

Citations

45 review citations

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

21 mentions without citation

BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions.
Behnke et al. (2015)
20 more