1C25

HUMAN CDC25A CATALYTIC DOMAIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.296 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.227 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A.

Fauman, E.B.Cogswell, J.P.Lovejoy, B.Rocque, W.J.Holmes, W.Montana, V.G.Piwnica-Worms, H.Rink, M.J.Saper, M.A.

(1998) Cell 93: 617-625

  • DOI: https://doi.org/10.1016/s0092-8674(00)81190-3
  • Primary Citation of Related Structures:  
    1C25

  • PubMed Abstract: 

    Cdc25 phosphatases activate the cell division kinases throughout the cell cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a small alpha/beta domain with a fold unlike previously described phosphatase structures but identical to rhodanese, a sulfur-transfer protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress. Asp-383, previously proposed to be the general acid, instead serves a structural role, forming a conserved buried salt-bridge. We propose that Glu-431 may act as a general acid. Structure-based alignments suggest that the noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein.


  • Organizational Affiliation

    Department of Biological Chemistry, The University of Michigan, Ann Arbor 48109-1055, USA. fauman@umich.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CDC25A161Homo sapiensMutation(s): 0 
Gene Names: CDC25A
EC: 3.1.3.48
UniProt & NIH Common Fund Data Resources
Find proteins for P30304 (Homo sapiens)
Explore P30304 
Go to UniProtKB:  P30304
PHAROS:  P30304
GTEx:  ENSG00000164045 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP30304
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.296 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.227 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.507α = 90
b = 43.507β = 90
c = 117.096γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-08-19
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references, Other