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The Open Protein Structure Annotation Network
PDB Keyword
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3bdv

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

    Title Crystal structure of YdeN-like protein of unknown function (DUF1234) (YP_051181.1) from Erwinia carotovora subsp. atroseptica SCRI1043 at 1.66 A resolution. To be published
    Site JCSG
    PDB Id 3bdv Target Id 379345
    Molecular Characteristics
    Source Erwinia carotovora subsp. atroseptica scri1043
    Alias Ids TPS1736,YP_051181.1, 104410 Molecular Weight 21802.56 Da.
    Residues 190 Isoelectric Point 5.08
    Sequence mqtteidlrltevsqqltmvlvpglrdsddehwqshwerrfphwqrirqrewyqadldrwvlairrels vctqpvilighsfgalaachvvqqgqegiagvmlvapaepmrfeiddriqasplsvptltfashndplm sftraqywaqawdselvdvgeaghinaeagfgpweyglkrlaefseilipnr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.66 Rfree 0.213
    Matthews' coefficent 1.96 Rfactor 0.170
    Waters 300 Solvent Content 37.15

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3bdv
    1. Ligands in PSI structures
    A Kumar, HJ Chiu, HL Axelrod, A Morse - Section F: Structural , 2010 - scripts.iucr.org
     
    2. CMASA: an accurate algorithm for detecting local protein structural similarity and its application to enzyme catalytic site annotation
    GH Li, JF Huang - BMC bioinformatics, 2010 - biomedcentral.com
     

    Protein Summary

    The ECA3091 gene from Erwinia carotovora atroseptica scri1043 encodes the YP_051181, a member of the DUF1234 group (PFAM:PF06821 COG:COG3545).

    3bdv structure adopts an alpha/beta hydrolase fold (SUNID:53473) and superfamily inside the alpha/beta class. According to DALI, 3bdv shows significant similarity to other homolog structures determined by structural genomics (PDB id: PDB:2qjw [Z=17], PDB:1uxo [Z=19], PDB:2i3d [Z=14], PDB:2gs9, and others annotated as esterases (Z=16) like PDB:1tqh, PDB:1r1d and PDB:1zoi.

    Analysis performed on a homologous and structurally similar hydrolase suggests this protein might be an esterase/lipase active on a soluble ester or small lipid [Ref].

    Ligand Summary


    References

    Reviews

    References

     

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