2FH7

Crystal structure of the phosphatase domains of human PTP SIGMA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.192 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Structural genomics of protein phosphatases.

Almo, S.C.Bonanno, J.B.Sauder, J.M.Emtage, S.Dilorenzo, T.P.Malashkevich, V.Wasserman, S.R.Swaminathan, S.Eswaramoorthy, S.Agarwal, R.Kumaran, D.Madegowda, M.Ragumani, S.Patskovsky, Y.Alvarado, J.Ramagopal, U.A.Faber-Barata, J.Chance, M.R.Sali, A.Fiser, A.Zhang, Z.Y.Lawrence, D.S.Burley, S.K.

(2007) J Struct Funct Genomics 8: 121-140

  • DOI: https://doi.org/10.1007/s10969-007-9036-1
  • Primary Citation of Related Structures:  
    1RXD, 2FH7, 2G59, 2HCM, 2HHL, 2HXP, 2HY3, 2I0O, 2I1Y, 2I44, 2IQ1, 2IRM, 2ISN, 2NV5, 2OYC, 2P27, 2P4U, 2P69, 2P8E, 2PBN, 2Q5E, 2QJC, 2R0B

  • PubMed Abstract: 

    The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.


  • Organizational Affiliation

    Albert Einstein College of Medicine, Bronx, NY, USA. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Receptor-type tyrosine-protein phosphatase S595Homo sapiensMutation(s): 0 
Gene Names: PTPRS
EC: 3.1.3.48
UniProt & NIH Common Fund Data Resources
Find proteins for Q13332 (Homo sapiens)
Explore Q13332 
Go to UniProtKB:  Q13332
PHAROS:  Q13332
GTEx:  ENSG00000105426 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ13332
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.192 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.333α = 90
b = 94.333β = 90
c = 123.036γ = 120
Software Package:
Software NamePurpose
SCALAdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
MOSFLMdata reduction
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-01-10
    Type: Initial release
  • Version 1.1: 2008-03-20
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-11-14
    Changes: Data collection, Structure summary
  • Version 1.4: 2021-02-03
    Changes: Database references, Structure summary
  • Version 1.5: 2023-08-30
    Changes: Data collection, Database references, Refinement description