5ND6

Crystal structure of apo transketolase from Chlamydomonas reinhardtii


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.58 Å
  • R-Value Free: 0.192 
  • R-Value Work: 0.159 
  • R-Value Observed: 0.161 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural basis for the magnesium-dependent activation of transketolase from Chlamydomonas reinhardtii.

Pasquini, M.Fermani, S.Tedesco, D.Sciabolini, C.Crozet, P.Naldi, M.Henri, J.Vothknecht, U.Bertucci, C.Lemaire, S.D.Zaffagnini, M.Francia, F.

(2017) Biochim Biophys Acta 1861: 2132-2145

  • DOI: https://doi.org/10.1016/j.bbagen.2017.05.021
  • Primary Citation of Related Structures:  
    5ND5, 5ND6

  • PubMed Abstract: 

    In photosynthetic organisms, transketolase (TK) is involved in the Calvin-Benson cycle and participates to the regeneration of ribulose-5-phosphate. Previous studies demonstrated that TK catalysis is strictly dependent on thiamine pyrophosphate (TPP) and divalent ions such as Mg 2+ .


  • Organizational Affiliation

    Department of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transketolase
A, B
693Chlamydomonas reinhardtiiMutation(s): 0 
Gene Names: TRK1CHLREDRAFT_141319
EC: 2.2.1.1
UniProt
Find proteins for A8IAN1 (Chlamydomonas reinhardtii)
Explore A8IAN1 
Go to UniProtKB:  A8IAN1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA8IAN1
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
EDO
Query on EDO

Download Ideal Coordinates CCD File 
C [auth A]1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.58 Å
  • R-Value Free: 0.192 
  • R-Value Work: 0.159 
  • R-Value Observed: 0.161 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 165.211α = 90
b = 74.311β = 119.3
c = 133.723γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
University of Bologna, Alma Mater StudiourumItalyFARB2012

Revision History  (Full details and data files)

  • Version 1.0: 2017-06-07
    Type: Initial release
  • Version 1.1: 2017-06-28
    Changes: Database references
  • Version 1.2: 2024-01-17
    Changes: Data collection, Database references, Refinement description