4F4B

Structure of OSH4 with a cholesterol analog

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.87 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.217 

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This is version 1.3 of the entry. See complete history. 


Literature

Synthesis and structure of 16,22-diketocholesterol bound to oxysterol-binding protein Osh4.

Koag, M.C., Cheun, Y., Kou, Y., Ouzon-Shubeita, H., Min, K., Monzingo, A.F., Lee, S.

(2013) Steroids 78: 938-944

  • DOI: https://doi.org/10.1016/j.steroids.2013.05.016
  • Primary Citation of Related Structures:  
    4F4B, 4FES

  • PubMed Abstract: 

    We have synthesized 16,22-diketocholesterol, a novel ligand for oxysterol-binding protein Osh4, and determined X-ray structure of the diketocholesterol in complex with Osh4. The X-ray structure shows that α7 helix of Osh4 assumes open conformation while the rest of Osh4, closed conformation, implying this diketocholesterol-bound Osh4 structure may represent a structural intermediate between the two conformations.

    • Organizational Affiliation: 

    Division of Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, TX 78712, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein KES1
A, B
436Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: KES1, OSH4, YPL145C, LPI3C, P2614
UniProt
Find proteins for P35844 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P35844 
Go to UniProtKB:  P35844
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP35844
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
L39
Query on L39
Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]		(3beta,9beta,25R)-3-hydroxy-26-iodocholest-5-ene-16,22-dione
C27 H41 I O3
AWHQELOUIOILMT-WQTURIIHSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.87 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.217 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 51.123α = 96.56
b = 65.397β = 100.28
c = 82.314γ = 95.91
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
BOSdata collection
HKL-2000data reduction
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-05-15
    Type: Initial release
  • Version 1.1: 2013-07-17
    Changes: Database references
  • Version 1.2: 2017-11-15
    Changes: Refinement description
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references, Derived calculations