2PQ5

Crystal structure of Dual specificity protein phosphatase 13 (DUSP13)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.176 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history. 


Literature

Crystal structure of Dual specificity protein phosphatase 13 (DUSP13).

Ugochukwu, E., Salah, E., Savitsky, P., Barr, A., Pantic, N., Niesen, F., Burgess-Brown, N., Berridge, G., Bunkoczi, G., Uppenberg, J., Pike, A.C.W., Sundstrom, M., Arrowsmith, C.H., Weigelt, J., Edwards, A., von Delft, F., Knapp, S.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dual specificity protein phosphatase 13
A, B, C, D
205Homo sapiensMutation(s): 0 
Gene Names: DUSP13, TMDP
EC: 3.1.3.48 (PDB Primary Data), 3.1.3.16 (PDB Primary Data)
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UII6 (Homo sapiens)
Explore Q9UII6 
Go to UniProtKB:  Q9UII6
PHAROS:  Q9UII6
GTEx:  ENSG00000079393 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UII6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.176 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.821α = 90
b = 73.821β = 90
c = 303.803γ = 120
Software Package:
Software NamePurpose
SHELXmodel building
SHELXL-97refinement
MAR345data collection
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-05-22
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2012-12-05
    Changes: Database references
  • Version 1.4: 2017-10-18
    Changes: Refinement description
  • Version 1.5: 2023-08-30
    Changes: Data collection, Database references, Refinement description