The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of a cysteine protease (BDI_2249) from Parabacteroides distasonis ATCC 8503 at 2.23 A resolution. To be published
    Site JCSG
    PDB Id 3pw3 Target Id 394726
    Molecular Characteristics
    Source Parabacteroides distasonis atcc 8503
    Alias Ids TPS25828,YP_001303602.1, 325963 Molecular Weight 43457.71 Da.
    Residues 382 Isoelectric Point 5.49
    Sequence dtekkvseegfvfttvkenpitsvknqnragtcwcyssysflesellrmgkgeydlsemftvyntyldr adaavrthgdvsfsqggsfydalygmetfglvpeeemrpgmmyadtlsnhtelsaltdamvaaiakgkl rklqsdennamlwkkavaavhqiylgvppekftykgkeytpksffestglkasdyvsltsythhpfytq fpleiqdnwrhgmsynlpldefmevfdnaintgytiawgsdvsesgftrdgvavmpddekvqelsgsdm ahwlklkpeekklntkpqpqkwctqaerqlaydnyettddhgmqiygiakdqegneyymvknswgtnsk yngiwyaskafvryktmnivvhkdalpkaikaklgik
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 3
    Resolution (Å) 2.23 Rfree 0.1812
    Matthews' coefficent 3.03 Rfactor 0.1592
    Waters 2007 Solvent Content 59.37

    Ligand Information



    Protein Summary

    First structure of bacterial  Peptidase C1B (PF03051), a member of bleomycin hydrolase family and a  Peptidase_CA (CL0125) clan. Multiple eukaryotic (yeast and human) structures were solved previously. Despite low sequence level similarity (~18% seq id) the structure is very similar to yeast bleomycin hydrolase and other cysteine proteinases. This family of peptidase functions as a hexamer.

    BDI_2249 is predicted to be secreted, possibly anchored in the outer membrane. Its exact function is unknown, possibly involved in extracellular protein degradation. Proteins from this family are abundant in all gut microbiome bacteroides, but also (more distant) in a wide variety of bacteria, with usually at least three paralogs in each genome. A distant homolog from S. thermophilus was purified and experimentally characterized [Ref].

    Ligand Summary




    1. (No Results)


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