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The Open Protein Structure Annotation Network
PDB Keyword
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2h0v

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

    Title Crystal structure of (2636545) from Bacillus subtilis at 2.60 A resolution. To be published
    Site JCSG
    PDB Id 2h0v Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1514,2636545, 2.60.120.10, 430152
    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 5.31 Rfactor 0.167
    Waters
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    Solvent Content 76.67

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2h0v
    1. Structural analysis of metal sites in proteins: non-heme iron sites as a case study
    C Andreini, I Bertini, G Cavallaro - Journal of molecular , 2009 - Elsevier
     

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    Protein Summary

    The gene yxaG (BSU39980) from Bacillus subtilis encodes the NP_391878 protein annotated, based on a BLAST search, as quercetin 2,3-dioxygenase ( EC:1.13.11.24). The enzyme contains two domains of the cupin superfamily PF07883 (bicupin).  

    The 2h0v structure belongs to the class of all beta proteins and adopts a double-stranded beta-helix fold type SCOP51181, inside the RmlC-like cupins superfamily, quercetin 2,3-dioxygenase-like family. The crystal structure of this enzyme (YxaG) has been independently solved by others (

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    [Ref]. DALI top hits are with quercetin dioxygenases
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    ,
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    and
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    (Z=37).

    The enzyme catalyzes the following reaction: Quercetin + O(2) <=> 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H(+).  It requires copper or iron ions as cofactors.  Common structural motifs, such as the cupin domains, are found in enzymes performing different biochemical functions while retaining a similar active site configuration and structural scaffold.   The bicupins, often suggested as products of gene duplication events,  have the potential to function as multienzymes, with each domain evolving to adopt a different functional role [Ref].

    Ligand Summary



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