4AHY

Flo5A cocrystallized with 3 mM GdAc3

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.185 

wwPDB Validation   3D Report Full Report


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


Literature

Complex Gadolinium-Oxo Clusters Formed Along Concave Protein Surfaces.

Veelders, M., Essen, L.-O.

(2012) Chembiochem 13: 2187

  • DOI: https://doi.org/10.1002/cbic.201200441
  • Primary Citation of Related Structures:  
    4AHW, 4AHX, 4AHY, 4AHZ, 4AI0, 4AI1, 4AI2, 4AI3

  • PubMed Abstract: 

    Protein-bound contrast: The unusual observation of a heptanuclear gadolinium-oxo cluster on the surface of the cell-adhesion protein Flo5A establishes the basis for directed incorporation of poly-lanthanide clusters into biomolecules. The observed gadolinium cluster might serve as a paradigm for the design of protein-based MRI contrast agents.

    • Organizational Affiliation: 

    Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Strasse, 35043 Marburg, Germany.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FLOCCULATION PROTEIN FLO5270Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P38894 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38894 
Go to UniProtKB:  P38894
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP38894
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.185 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.3α = 90
b = 61.76β = 90
c = 106.08γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
REFMACphasing

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-10-03
    Type: Initial release
  • Version 1.1: 2012-10-31
    Changes: Database references
  • Version 1.2: 2017-06-28
    Changes: Data collection
  • Version 1.3: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description