› 2llv

Solution NMR

Solution structure of the yeast Sti1 DP1 domain

Released:
DOI: 10.2210/pdb2llv/pdb
PDB entry 2llv coloured by chain, ensemble of 21 models, front view.
PDB entry 2llv coloured by chain, ensemble of 21 models, side view.
PDB entry 2llv coloured by chain, ensemble of 21 models, 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147469 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein STI1 Chain: A
Molecule details ›
Chain: A
Length: 71 amino acids
Theoretical weight: 7.94 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15705 (Residues: 127-197; Coverage: 12%)
Gene names: OR26.17, STI1, YOR027W
Sequence domains: STI1/HOP, DP domain
Structure domains: 434 Repressor (Amino-terminal Domain)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 94%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

32 review citations

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

5 mentions without citation

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