› 4inq

X-ray diffraction
2.2Å resolution

Crystal structure of Osh3 ORD in complex with PI(4)P from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb4inq/pdb
PDB entry 4inq coloured by chain, front view.
PDB entry 4inq coloured by chain, side view.
PDB entry 4inq 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

1 bound ligand:
Ligand PIF 1 x PIF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P212121
Unit cell:
a: 39.889Å b: 88.992Å c: 95.665Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.28
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

4 mentions without citation

Structural basis of substrate specificity and protease inhibition in Norwalk virus.
Muhaxhiri et al. (2013)
3 more