3F0N

Mus Musculus Mevalonate Pyrophosphate Decarboxylase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of Mus Musculus Mevalonate Pyrophosphate Decarboxylase

Walker, J.R.Davis, T.Vesterberg, A.Li, Y.Bountra, C.Weigelt, J.Arrowsmith, C.H.Edwards, A.M.Bochkarev, A.Dhe-Paganon, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MEVALONATE PYROPHOSPHATE DECARBOXYLASE
A, B
414Mus musculusMutation(s): 2 
Gene Names: MVD
EC: 4.1.1.33
UniProt & NIH Common Fund Data Resources
Find proteins for Q99JF5 (Mus musculus)
Explore Q99JF5 
Go to UniProtKB:  Q99JF5
IMPC:  MGI:2179327
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ99JF5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 139.619α = 90
b = 139.619β = 90
c = 88.719γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2008-11-25
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description