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1ydo

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

    Title Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds. J.Biol.Chem. 281 7533-7545 2006
    Site NESGC
    PDB Id 1ydo Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS9071,PF00682, 3.20.20.70
    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 2.40 Rfactor 0.263
    Waters
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    Solvent Content 45.00

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    Ligand Information
    Ligands
    Metals IOD (IODIDE) x 4

    Jmol

     
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    Google Scholar output for 1ydo
    1. Molecular genetics of HMG-CoA lyase deficiency
    J Pi, E Lopez-Vinas, B Puisac, S Menao, A Pi - Molecular genetics and , 2007 - Elsevier
     
    2. Strategies for high_throughput comparative modeling: Applications to leverage analysis in structural genomics and protein family organization
    N Mirkovic, Z Li, A Parnassa - : Structure, Function, and , 2007 - Wiley Online Library
     
    3. Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes
    F Forouhar, M Hussain, R Farid, J Benach - Journal of Biological , 2006 - ASBMB
     
    4. MDockPP: A hierarchical approach for protein_protein docking and its application to CAPRI rounds 1519
    SY Huang, X Zou - Proteins: Structure, Function, and , 2010 - Wiley Online Library
     
    5. C-Terminal end and aminoacid Lys 48 in HMG-CoA lyase are involved in substrate binding and enzyme activity
    P Carrasco, S Menao, E Lopez-Vinas - Molecular genetics and , 2007 - Elsevier
     

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    Protein Summary


    Ligand Summary

    Reviews

    References

     

    No references found.

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