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 STRUCTURAL GENOMICS, UNKNOWN FUNCTION (BACOVA_03430) from Bacteroides ovatus at 2.40 A resolution. To be published
    Site JCSG
    PDB Id 3n91 Target Id 416727
    Molecular Characteristics
    Source Bacteroides ovatus atcc 8483
    Alias Ids TPS33825,ZP_02066433.1, 384457 Molecular Weight 35908.40 Da.
    Residues 322 Isoelectric Point 4.99
    Sequence sdnefpdfdyqtvyfanqyglrtielgesefvdntldnqhkmvikaawgggytnrnnvvinfkvdeslc dnlyfkdtdqplvpmpasyytlasdriaipkgqimagvevqltddffadeksisenyvipllmtnvqga dsilqgkpvvenpvltnagdwsilpqnfvlyavkyvnpwhgeylrrgidhatvagtskdiirheqfven devvnistksmkdnlltlktkdesgkdisytvrlsfaedgsctvhsgsqnvvvsgsgkfvskgeknslg gkdrnaiyldytvnltdnniqlatkdtlvlrtrnvyggkslevvrk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.40 Rfree 0.220
    Matthews' coefficent 3.62 Rfactor 0.181
    Waters 179 Solvent Content 65.99

    Ligand Information


    Google Scholar output for 3n91
    1. Blind prediction of quaternary structures of homo-oligomeric proteins from amino acid sequences based on templates
    M Morita, M Kakuta, K Shimizu, S Nakamura - 2012 - hoajonline.com

    Protein Summary

    ZP_02066433.1 (BACOVA_03430) is a screted protein which can be divided into two domains: d1 (residues 30-196+333-344 ), and d2 (197-332). D2 is homologous to another jcsg structure 3h3i (Dali Z=10.2 for rmsd of 3.2A for 108 aligned Ca, seq id 14%). Other similar structures to D2 include: outer membrane protein W (2f1v), 2erv, and avidin (1ldo). D1 shares similar to NA/CA exchange protein (pdb 3e9u, Z=9.7), integrin beta-4 (pdb 3fso, Z=9.2).


    Based on annotations of sequence homologs in the database, this protein could be adhesin-like. Sequence analysis indicated that D1 matches DUF1735, which is related to another jcsg structure (416718).


    Fig 1.  Monomer of ZP_02066433.1


    Ligand Summary




    No references found.

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