4M2A

Crystal structure of the udp-glucose pyrophosphorylase from Leishmania major in the post-reactive state


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.66 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.190 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Catalytic Mechanism and Allosteric Regulation of Udp-Glucose Pyrophosphorylase from Leishmania Major

Fuehring, J.Routier, F.H.Lamerz, A.-C.Baruch, P.Gerardy-Schahn, R.Fedorov, R.

(2013) ACS Catal 3: 2161-2985


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UDP-glucose pyrophosphorylase505Leishmania majorMutation(s): 0 
Gene Names: LMJF_18_0990UGP
EC: 2.7.7.9
UniProt
Find proteins for Q4QDU3 (Leishmania major)
Explore Q4QDU3 
Go to UniProtKB:  Q4QDU3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4QDU3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.66 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.190 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.79α = 90
b = 89.09β = 90
c = 136.49γ = 90
Software Package:
Software NamePurpose
CCP4model building
CNSrefinement
XDSdata reduction
SADABSdata scaling
CCP4phasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-01-29
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description