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The Open Protein Structure Annotation Network
PDB Keyword
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2f46

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 A resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases. Proteins 69 415-421 2007
    Site JCSG
    PDB Id 2f46 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1508,7380613, PF04273
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.01 Rfactor 0.2
    Waters
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    Solvent Content 38.69

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2f46
    1. Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 resolution provides a structural scaffold for nonclassical, eukaryotic_like phosphatases
    S Krishna, L Tautz, Q Xu, D McMullan - Proteins: Structure, , 2007 - Wiley Online Library
     
    2. The highest reflection intensity in a resolution shell
    M Bochtler, G Chojnowski - Acta Crystallographica Section A: , 2007 - scripts.iucr.org
     
    3. Protein tyrosine phosphatase structurefunction relationships in regulation and pathogenesis
    F Bhmer, S Szedlacsek, L Tabernero, A stman - FEBS , 2012 - Wiley Online Library
     
    4. The statistics of the highest E value
    G Chojnowski, M Bochtler - Acta Crystallographica Section A: , 2007 - scripts.iucr.org
     

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    Protein Summary

    The gene NMA1982 from Neisseria meningitidis z2491 encodes the YP_002343251 protein, a  putative tyrosine phosphatase from the DUF442 family (PF04273).  

    The 2f46 structure belongs to the class of alpha and beta (a+b) proteins and adopts a phosphotyrosine protein phosphatases II  fold type SCOP52798.  DALI top hits are with cyclin dependent kinase inhibitor-3 protein

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    (Z=15),
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    (Z=14), the DUF442 protein
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    (Z=14) and the phosphatase
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    (Z=14). A similar structure from Arabidopsis thaliana has been determined
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    (Z=14).  The phosphatase activity of the enzyme was confirmed in vitro [Ref].  The overall fold of this phosphatase resembles that of eukaryotic-like phosphatases, PTP1B in particular
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    (Z=8).  

    N. meningitidis is an important human pathogen responsible for causing meningitis and septicaemia, which are debilitating diseases that kill thousands of people every year.  Thus, this phosphatase might be a very promising target for therapeutic intervention.

    Ligand Summary



    References

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