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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 367501
    Molecular Characteristics
    Source Bacillus subtilis subsp. subtilis str. 168
    Alias Ids TPS1514,2636545, 2.60.120.10, 430152 Molecular Weight 37582.69 Da.
    Residues 337 Isoelectric Point 5.61
    Sequence mktlcthslpkekmpyllrsgegerylfgrqvatvmangrstgdlfeivllsggkgdafplhvhkdthe gilvldgkleltldgeryllisgdyanipagtphsyrmqshrtrlvsytmkgnvahlysvignpydhae hppyaseevsnerfaeaaavativfldeakpacsaklaeltelpdgavpyvlesgegdrlltgdqlhri vaaqkntdgqfivvssegpkgdrivdhyheyhtetfyclegqmtmwtdgqeiqlnpgdflhvpantvhs yrldshytkmvgvlvpglfepffrtlgdpyeghifpckpqalrfdrilqniealdlkvmkp
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.60 Rfree 0.204
    Matthews' coefficent 5.31 Rfactor 0.167
    Waters 312 Solvent Content 76.67

    Ligand Information
    Ligands
    Metals

    Jmol

     
    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
     

    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 (PDB:1y3t [Ref]. DALI top hits are with quercetin dioxygenases PDB:1h1i, PDB:1gqg and PDB:1juh (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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