› 4ic4

X-ray diffraction
1.5Å resolution

Crystal structure of Osh3 ORD from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb4ic4/pdb
PDB entry 4ic4 coloured by chain, front view.
PDB entry 4ic4 coloured by chain, side view.
PDB entry 4ic4 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins.
Tong J, Yang H, Yang H, Eom SH, Im YJ
Structure 21 1203-13 (2013)
PMID: 23791945

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxysterol-binding protein homolog 3 Chain: A
Molecule details ›
Chain: A
Length: 397 amino acids
Theoretical weight: 45.68 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P38713 (Residues: 605-996; Coverage: 39%)
Gene names: OSH3, YHR073W
Sequence domains: Oxysterol-binding protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 40.866Å b: 89.2Å c: 96.102Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.234
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.
Wong et al. (2019)
24 more

2 mentions without citation

Allosteric enhancement of ORP1-mediated cholesterol transport by PI(4,5)P2/PI(3,4)P2.
Dong et al. (2019)
1 more