4OPN

Crystal structure of mouse glyoxalase I complexed with mAH


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.231 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.180 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Reversible Inhibition of Glyoxalase I: Synthesis and Activity Evaluation

Shi, Q.Zhai, J.Zheng, Z.Hu, X.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lactoylglutathione lyase
A, B
184Mus musculusMutation(s): 0 
Gene Names: Glo1
EC: 4.4.1.5
UniProt
Find proteins for Q9CPU0 (Mus musculus)
Explore Q9CPU0 
Go to UniProtKB:  Q9CPU0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9CPU0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.231 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.180 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.559α = 90
b = 65.084β = 101.29
c = 64.885γ = 90
Software Package:
Software NamePurpose
CrysalisProdata collection
MOLREPphasing
PHENIXrefinement
CrysalisProdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-02-11
    Type: Initial release
  • Version 1.1: 2024-03-20
    Changes: Data collection, Database references, Derived calculations