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1vmk

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

    Title Crystal structure of Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima at 2.01 A resolution. To be published
    Site JCSG
    PDB Id 1vmk Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1302,TM1596, 282594
    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 3
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.56 Rfactor 0.20391
    Waters
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    Solvent Content 51.64

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vmk
    1. PNP anticancer gene therapy
    Y Zhang, WB Parker, EJ Sorscher - Current topics in , 2005 - ingentaconnect.com
     
    2. Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from
    HM Pereira, MM Rezende, MS Castilho - Section D: Biological , 2009 - scripts.iucr.org
     
    3. Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing
    R Guan, MC Ho, SC Almo, VL Schramm - Biochemistry, 2011 - ACS Publications
     

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    Protein Summary

    Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima catalyzes the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.

    There are several similar proteins with known structure, for example: 1c3xA, 1a9o, 1pf7E, 1tcuA, 1yqqA, 1g2oA, 2a8yA, 1v4nA, 1cb0A, and 1wtaA.

    TM1596 has phosphorylase/hydrolase-like fold (SCOP sunid 53162) core: 3 layers, ?/?/?; mixed sheet of 5 strands: order 21354; strand 4 is antiparallel to the rest; contains crossover loops.

    Ligand Summary



    References

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