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The Open Protein Structure Annotation Network
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1p91

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

    Title Crystal structure of RlmAI: implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site. Proc.Natl.Acad.Sci.Usa 101 4041-4046 2004
    Site NESGC
    PDB Id 1p91 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS8834,PF01209, PF08241, PF02390, PF05175, 3.40.50.150
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.81 Rfactor 0.248
    Waters
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    Solvent Content 67.68

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    Ligand Information
    Ligands SO4 (SULFATE) x 5;SAM (S-ADENOSYLMETHIONINE) x 2
    Metals ZN (ZINC) x 2

    Jmol

     
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    Google Scholar output for 1p91
    1. Crystal structure of RlmAI: implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site
    K Das, T Acton, Y Chiang, L Shih - Proceedings of the , 2004 - National Acad Sciences
     
    2. Performance of ZDOCK and ZRANK in CAPRI rounds 1319
    H Hwang, T Vreven, BG Pierce - Proteins: Structure, , 2010 - Wiley Online Library
     
    3. Conformational changes in redox pairs of protein structures
    SW Fan, RA George, NL Haworth, LL Feng - Protein , 2009 - Wiley Online Library
     
    4. A generalized approach to sampling backbone conformations with RosettaDock for CAPRI rounds 1319
    A Sircar, S Chaudhury, KP Kilambi - Proteins: Structure, , 2010 - Wiley Online Library
     
    5. 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
     
    6. Protein Structure Database for Structural Genomics Group
    JY Lau - 2005 - www-nmr.cabm.rutgers.edu
     

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    Protein Summary


    Ligand Summary

    Reviews

    References

     

    No references found.

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