2I1Y

Crystal structure of the phosphatase domain of human PTP IA-2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.23 Å
  • R-Value Free: 0.267 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.201 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.4 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
A, B
301Homo sapiensMutation(s): 0 
Gene Names: PTPRNICA3ICA512
EC: 3.1.3.48
UniProt & NIH Common Fund Data Resources
Find proteins for Q16849 (Homo sapiens)
Explore Q16849 
Go to UniProtKB:  Q16849
PHAROS:  Q16849
GTEx:  ENSG00000054356 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ16849
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.23 Å
  • R-Value Free: 0.267 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.201 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.907α = 90
b = 74.229β = 90
c = 121.067γ = 90
Software Package:
Software NamePurpose
MOLREPphasing
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-08-29
    Type: Initial release
  • Version 1.1: 2008-03-20
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2021-02-03
    Changes: Advisory, Database references, Derived calculations, Structure summary
  • Version 1.4: 2023-08-30
    Changes: Advisory, Data collection, Database references, Refinement description