4N9N

Crystal Structure of Saccharomyces cerevisiae Upc2 Transcription Factor fused with T4 Lysozyme


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.251 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural mechanism of ergosterol regulation by fungal sterol nuclear receptor Upc2

Yang, H.Tong, J.Ha, S.Eom, S.H.Im, Y.J.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Sterol uptake control protein 2, Lysozyme
A, B
438Saccharomyces cerevisiae S288CTequatrovirus T4Mutation(s): 2 
Gene Names: UPC2E
EC: 3.2.1.17
UniProt
Find proteins for Q12151 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q12151 
Go to UniProtKB:  Q12151
Find proteins for P00720 (Enterobacteria phage T4)
Explore P00720 
Go to UniProtKB:  P00720
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP00720Q12151
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.251 
  • Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.17α = 90
b = 67.17β = 90
c = 257.51γ = 120
Software Package:
Software NamePurpose
ADSCdata collection
SOLVEphasing
CNSrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-12-03
    Type: Initial release
  • Version 1.1: 2017-08-16
    Changes: Refinement description, Source and taxonomy
  • Version 1.2: 2024-11-20
    Changes: Data collection, Database references, Derived calculations, Structure summary