2HY3

Crystal structure of the human tyrosine receptor phosphate gamma in complex with vanadate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.288 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.206 

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. almo@aecom.yu.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Receptor-type tyrosine-protein phosphatase gamma
A, B
313Homo sapiensMutation(s): 7 
Gene Names: PTPRG
EC: 3.1.3.48
UniProt & NIH Common Fund Data Resources
Find proteins for P23470 (Homo sapiens)
Explore P23470 
Go to UniProtKB:  P23470
PHAROS:  P23470
GTEx:  ENSG00000144724 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP23470
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.288 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.206 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.173α = 90
b = 74.787β = 99.58
c = 82.071γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data collection
HKL-2000data reduction
SCALEPACKdata scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-09-05
    Type: Initial release
  • Version 1.1: 2008-03-20
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2018-11-14
    Changes: Data collection, Structure summary
  • Version 1.4: 2021-02-03
    Changes: Database references, Derived calculations, Structure summary