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2f8l

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

    Title Crystal structure of (16411011) from Listeria monocytogenes LI2 at 2.20 A resolution. To be published
    Site JCSG
    PDB Id 2f8l Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1422,16411011, 432863
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.75 Rfactor 0.165
    Waters
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    Solvent Content 66.92

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2f8l
    1. MarkUs: a server to navigate sequencestructurefunction space
    M Fischer, QC Zhang, F Dey, BY Chen - Nucleic Acids , 2011 - Oxford Univ Press
     

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    Protein Summary

    The gene lmo1582 from Listeria monocytogenes encodes the NP_465107 protein, a putative S-adenosylmethionine-dependent methyltransferase (SAM or AdoMet-MTase) class I, a member of N-6 DNA methylase-like family PF02384. The enzyme belongs to the class of alpha and beta (a+b) proteins and reveals S-adenosyl-L-methionine-dependent methyltransferases fold type SCOP53334.  AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.). 

    Ligand Summary



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