2CZ2

Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from Mus musculus (form-1 crystal)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.196 
  • R-Value Work: 0.155 
  • R-Value Observed: 0.157 

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This is version 1.2 of the entry. See complete history


Literature

Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from Mus musculus (form-1 crystal)

Mizohata, E.Morita, S.Kinoshita, Y.Nagano, K.Uda, H.Uchikubo, T.Shirouzu, M.Yokoyama, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Maleylacetoacetate isomerase223Mus musculusMutation(s): 6 
EC: 5.2.1.2 (PDB Primary Data), 2.5.1.18 (PDB Primary Data)
UniProt
Find proteins for Q9WVL0 (Mus musculus)
Explore Q9WVL0 
Go to UniProtKB:  Q9WVL0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9WVL0
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.196 
  • R-Value Work: 0.155 
  • R-Value Observed: 0.157 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.967α = 90
b = 152.134β = 90
c = 57.051γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-01-10
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance