3gl1

X-ray diffraction
1.92Å resolution

Crystal structure of ATPase domain of Ssb1 chaperone, a member of the HSP70 family, from Saccharomyces cerevisiae

Released:
Source organism: Saccharomyces cerevisiae
Entry authors: Osipiuk J, Li H, Bargassa M, Sahi C, Craig EA, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosome-associated molecular chaperone SSB1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 387 amino acids
Theoretical weight: 42.1 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P11484 (Residues: 1-384; Coverage: 63%)
Gene names: SSB1, YDL229W, YG101
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 76.543Å b: 54.504Å c: 90.623Å
α: 90° β: 104.36° γ: 90°
R-values:
R R work R free
0.167 0.164 0.218
Expression system: Escherichia coli