3dm7

X-ray diffraction
2Å resolution

Crystal Structure of the Vps75 Histone Chaperone

Released:
Model geometry
Fit model/data
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of Vps75 and implications for histone chaperone function.
Proc Natl Acad Sci U S A 105 12206-11 (2008)
PMID: 18723682

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-156889 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar protein sorting-associated protein 75 Chains: A, B
Molecule details ›
Chains: A, B
Length: 234 amino acids
Theoretical weight: 27.8 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53853 (Residues: 1-232; Coverage: 88%)
Gene names: N0890, VPS75, YNL246W
Sequence domains: Nucleosome assembly protein (NAP)

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 79.01Å b: 89.658Å c: 94.069Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.24
Expression system: Escherichia coli