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Crystal structure of OSH3 ord in complex with PI(4)P from saccharomyces cerevisiae

Analyse Crystal structure of OSH3 ord in complex with PI(4)P from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4INQ
Type
protein
Length
372 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Oxysterol-binding protein homolog 3
UniProt
P38713
Ligands
PIF
Pockets
3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOxysterol-binding protein homolog 3protein37225% helix, 30% strandP38713

Ligands and binding sites

  • PIF · (2R)-3-{[(S)-hydroxy{[(1r,2r,3r,4r,5s,6r)-2,3,5,6-tetrahydroxy-4-(phosphonooxy) cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dioctanoate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17410.830.8665PIF
2690.320.7521empty
3600.280.7314empty

Compared structures

  • 4INQ · Crystal structure of Osh3 ORD in complex with PI(4)P from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
  • P38713 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein homolog 3 (P38713) · a predicted model of the same protein · chain A against A, TM-score 0.99

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