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The Open Protein Structure Annotation Network
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3n0w

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

    Title Crystal structure of a branched chain amino acid ABC transporter periplasmic ligand-binding protein (Bxe_C0949) from BURKHOLDERIA XENOVORANS LB400 at 1.88 A resolution. To be published
    Site JCSG
    PDB Id 3n0w Target Id 396222
    Molecular Characteristics
    Source Burkholderia xenovorans lb400
    Alias Ids TPS25398,YP_556174.1, BIG_798, 384389 Molecular Weight 40819.44 Da.
    Residues 378 Isoelectric Point 9.10
    Sequence qstgqvtlgvltdmssvyadsagkgsvaavqlaiedvggkalgqpvklvsadyqmktdvalsiarewfd rdgvdaifdvvnsgtalainnlvkdkkklafitaaaadqiggtecngygigflynftsivktvvqaqla kgyktwflmlpdaaygdlmnaairreltagggqivgsvrfpfetqdfssyllqakasgaqlivstsgga aninimkqarefglpsktqkvggmidiltdvksaglrvmqgqeyatsfywnmddrtrafakrfyakmgk mptnnqaggysaalqylkavnaigskdpqkvfaylktikfddavtrhgtlrpggrlvrdmylvrakkpe dqkgdwdyydvvatigpeqafgplsesrcamdk
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.88 Rfree 0.233
    Matthews' coefficent 2.45 Rfactor 0.191
    Waters 732 Solvent Content 49.74

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3n0w
    1. Predicting protein ligand binding motions with the Conformation Explorer
    SC Flores, MB Gerstein - BMC bioinformatics, 2011 - biomedcentral.com
     

    Protein Summary

    The following content is uploaded from Kevin Kai Jin's refinement summary, more discussion about these Eut protein structures will be continuously added very soon.

    Pfam update: On building, this rapidly overlapped with ANF_receptor PF01094.

    Gene YP_556174.1 encodes a protein with 399residues from Burkholderia xenovorans lb400 with Isoelectric Point of 9.17, which belongs to PF01094 receptor family ligand binding region.  The NCI blast sequence alignment also indicates that this protein carries putative conserved domains belonging to the superfamily of type 1 periplasmic binding protein.   A structural homolog search via SSM and Dali sever show that this protein is a structural homolog to those ABC protein structures.  The interface interaction suggests that the biomolecule of this protein be a dimer. 
     
    396222_1.png

     

    Figure 1. Protein YP_556174.1 is monomer for its biomolecule assignment.

     

    396222_3.png

     

    Figure 2. Protein YP_556174  is structural homolog

    to AMIDASE OPERON (PDB ID 1PEA, magenta) and

    another ABC protein from JCSG (PDB ID 3I09,yellow).

     

     

    396222_2.png

     

    Figure 3. Protein YP_556174 consists of two domains.

    Based on its function annotation, part of density at domain

    interface is modeled as the phosphate moiety from ADP.

     

     

    References,

    1.    Kuryatov A, Laube B, Betz H, Kuhse J; , Neuron 1994;12:1291-1300.: Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins.

     

     

     

    Ligand Summary

    Reviews

    References

     

    No references found.

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