Oxysterol-binding protein homolog

spinqualitylabelsall models Yeast oxysterol-binding protein homolog 4 complex with cholesterol and Pb+2 ion (black) (PDB code 1zhy) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Oxysterol-binding protein homolog (Osh) mediate sterol transport from the ER to mitochondria. Sterols are synthesized in the ER and are present in membranes and affect the membrane fluidity and permeability. Osh4 or Kes1 is involved in membrane and lipid trafficking through trans-Golgi network and endosomal systems. Structural highlights The structure of the complex between Osh4 and cholesterol shows the cholesterol binding in a tunnel covered by a lid formed by the protein N-terminal with the ligand forming numerous interactions with Osh4. Water molecules are shown as red spheres.

3D structures of oxysterol-binding protein homolog

Updated on 13-April-2026

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• Osh1
  • 5h28 – yOsh1 ANK domain - yeast
    
  • 5h2c – yOsh1 ANK domain + nucleus-vacuole junction protein
    
  • 5h2d – yOsh1 ORD domain + ergosterol
    
  • 5wvr – yOsh1 ORD domain + cholesterol
    
  • 5h2a – Osh1 ANK domain – Kluyveromyces lactis
    
• Osh3
  • 4iap – yOsh3 PH domain
    
  • 4ic4 – yOsh3 OSBP-related domain
    
  • 4inq – yOsh3 OSBP-related domain + phosphoinositide
    
• Osh4 or KES1
  • 1zi7 – yOsh4 (mutant)
    
  • 1zht, 1zhw, 1zhx – yOsh4 + hydroxycholesterol derivative
    
  • 1zhy – yOsh4 + cholesterol
    
  • 1zhz – yOsh4 + ergosterol
    
  • 4jch – yOsh4 + oxysterol
    
  • 4f4b, 4fes – yOsh4 + cholesterol analog
    
  • 3spw – yOsh4 + phosphatidylinositol phosphate
    
• Osh6
  • 4b2z – yOsh6 + phosphatidylserine
    
  • 4ph7 – yOsh6 + phosphatidylinositol phosphate
    
  • 9hdh, 9hdk – yOsh6 + IST2 + POPS
    

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