› 3uq3

X-ray diffraction
2.6Å resolution

TPR2AB-domain:pHSP90-complex of yeast Sti1

Released:
DOI: 10.2210/pdb3uq3/pdb
PDB entry 3uq3 coloured by chain, front view.
PDB entry 3uq3 coloured by chain, side view.
PDB entry 3uq3 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.
Schmid AB, Lagleder S, Gräwert MA, Röhl A, Hagn F, Wandinger SK, Cox MB, Demmer O, Richter K, Groll M, Kessler H, Buchner J
EMBO J 31 1506-17 (2012)
PMID: 22227520

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140053 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heat shock protein STI1 Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 29.34 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15705 (Residues: 262-515; Coverage: 43%)
Gene names: OR26.17, STI1, YOR027W
Sequence domains: Tetratricopeptide repeat
Structure domains: Tetratricopeptide repeat domain
Heat shock protein HSP 90-beta Chains: B, C
Molecule details ›
Chains: B, C
Length: 5 amino acids
Theoretical weight: 622 Da
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P08238 (Residues: 720-724; Coverage: 1%)
Gene names: HSP90AB1, HSP90B, HSPC2, HSPC3, HSPCB

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 43.191Å b: 62.897Å c: 66.842Å
α: 90° β: 95.8° γ: 90°
R-values:
R R work R free
0.22 0.217 0.279
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

32 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
31 more

9 mentions without citation

Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery.
Wang et al. (2020)
8 more