RCSB PDB - 5ESL: Saccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) T322I mutant complexed with itraconazole

 5ESL

Saccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) T322I mutant complexed with itraconazole


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.212 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted 1YNClick on this verticalbar to view detailsBest fitted HEMClick on this verticalbar to view details

This is version 1.3 of the entry. See complete history


Literature

Structures of lanosterol 14-alpha demethylase mutants.

Sagatova, A.Keniya, M.V.Wilson, R.K.Sabherwal, M.Tyndall, J.D.A.Monk, B.C.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lanosterol 14-alpha demethylase539Saccharomyces cerevisiae YJM789Mutation(s): 1 
Gene Names: ERG11SCY_2394
Membrane Entity: Yes 
UniProt
Find proteins for A6ZSR0 (Saccharomyces cerevisiae (strain YJM789))
Explore A6ZSR0 
Go to UniProtKB:  A6ZSR0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA6ZSR0
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
1YN
Query on 1YN

Download Ideal Coordinates CCD File 
B [auth A]2-[(2R)-butan-2-yl]-4-{4-[4-(4-{[(2R,4S)-2-(2,4-dichlorophenyl)-2-(1H-1,2,4-triazol-1-ylmethyl)-1,3-dioxolan-4-yl]methoxy}phenyl)piperazin-1-yl]phenyl}-2,4-dihydro-3H-1,2,4-triazol-3-one
C35 H38 Cl2 N8 O4
VHVPQPYKVGDNFY-DFMJLFEVSA-N
HEM
Query on HEM

Download Ideal Coordinates CCD File 
C [auth A]PROTOPORPHYRIN IX CONTAINING FE
C34 H32 Fe N4 O4
KABFMIBPWCXCRK-RGGAHWMASA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.212 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.09α = 90
b = 65.39β = 98.42
c = 80.78γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
Blu-Icedata collection
Aimlessdata scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted 1YNClick on this verticalbar to view detailsBest fitted HEMClick on this verticalbar to view details

Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Health Research Council (HRC)New Zealand--
Marsden FundNew Zealand--

Revision History  (Full details and data files)

  • Version 1.0: 2016-11-23
    Type: Initial release
  • Version 1.1: 2017-09-20
    Changes: Author supporting evidence, Data collection
  • Version 1.2: 2020-01-01
    Changes: Author supporting evidence
  • Version 1.3: 2023-09-27
    Changes: Data collection, Database references, Refinement description