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The Open Protein Structure Annotation Network
PDB Keyword
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3cea

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

    Title Crystal structure of myo-inositol 2-dehydrogenase (NP_786804.1) from Lactobacillus plantarum at 2.40 A resolution. To be published
    Site JCSG
    PDB Id 3cea Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1741,NP_786804.1, 452589
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 4
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.23 Rfactor 0.193
    Waters
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    Solvent Content 44.84

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3cea
    1. PSI-2: structural genomics to cover protein domain family space
    BH Dessailly, R Nair, L Jaroszewski, JE Fajardo - Structure, 2009 - Elsevier
     
    2. Structure-activity relationships in peptide-antibody complexes: implications for epitope prediction and development of synthetic peptide vaccines
    SW Chen, MHV Van Regenmortel - Current medicinal , 2009 - ingentaconnect.com
     
    3. Docking and biomolecular simulations on computer Grids: status and trends
    AA Tantar, S Conilleau, B Parent - -Aided Drug Design, 2008 - ingentaconnect.com
     
    4. Structure and RNA interactions of the plant microRNA processing associated protein HYL1
    RM Rasia, J Mateos, NG Bologna, P Burdisso - Biochemistry, 2010 - ACS Publications
     
    5. A novel _-N-acetylgalactosaminidase family with an NAD+-dependent catalytic mechanism suitable for enzymatic removal of blood group A antigens
    G Sulzenbacher, QP Liu, EP Bennett - Biocatalysis and , 2009 - informahealthcare.com
     
    6. The cell surface proteoglycans syndecan-1 and-4 bind overlapping but distinct sites in the laminin _3 LG45 domain
    S Carulli, K Beck, G Dayan, S Boulesteix - Journal of Biological , 2012 - ASBMB
     
    7. Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification
    K van Straaten, H Zheng, D Palmer, D Sanders - Biochem. J, 2010 - biochemj.org
     
    8. Best Abstracts
    C Lenormand, F Gross, H Bausinger, D Fricker - 2011 - Wiley Online Library
     

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    Protein Summary

    This protein, myo-inositol 2-dehydrogenase, belongs to the PFAM family of PF01408; GFO_IDH_MocA. The biomolecule is tetramer. Each monomer has a fold common to Oxidoreductase, but the tetramer orients such that two long sheets form a channel of some sort with helices on either side of the channel. The flanking domain adopts the oxidoreductase fold.

    Fig.1 Tetramer showing one NAD bound to each monomer.

     
    Fig. 2 Two orthogonal views showing a channel formed by beta sheets.

    The monomer has a common fold with several homologs in the PDB (e.g. 2GLX 1OFG 1ZH8 2IXA 2NVW 2P2S 1YDW 1TLT 1GCU 2HO3 1XEA). Of these, 2GLX, 1OFG, 1ZH8 ,2IXA,  2P2S  also have NAD bound to them in identical location.

    Ligand Summary

    NAD is bound to the protein.

    References

    Reviews

    References

     

    No references found.

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