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The Open Protein Structure Annotation Network
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3iht

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

    Title Crystal structure of S-adenosyl-L-methionine methyl transferase (YP_165822.1) from SILICIBACTER POMEROYI DSS-3 at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 3iht Target Id 392348
    Molecular Characteristics
    Source Silicibacter pomeroyi dss-3
    Alias Ids TPS24425,YP_165822.1, 323685 Molecular Weight 19326.02 Da.
    Residues 173 Isoelectric Point 6.23
    Sequence mremqimsqpeqsrldlfidrmvsqraclehaiaqtaglsgpvyelglgngrtyhhlrqhvqgreiyvf eravashpdstppeaqlilgdiretlpatlerfgataslvhadlgghnrekndrfarlispliephlaq gglmvssdrmyfegleelplppgavvgrcfiyrrg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.80 Rfree 0.194
    Matthews' coefficent 2.99 Rfactor 0.173
    Waters 314 Solvent Content 58.92

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3iht

    Protein Summary

    This protein is likely a methytransferase, as evident by the bound SAM ligand and structural similarity to other methyltransferase. The SAM is well definied in one monomer but very low occ in the second monomer in the asu.

     

    Note from PFam:

    This protein didn't match any Pfam families. I have built a new Pfam entry from this sequence and it is called Methyltransf_17 (PF12692). This is the first structure for the family. I have added the family to the NADP_Rossmann clan (CL0063) for which there are already lots of structures known.

     

    Figure 1. dimer with SAM in one monomer

    FR15172a-dimer.png

    Figure 2. comparison with 2nyu (e coli human FtsJ homolog---RNA methyltransferase)

    2nyu-fr15172a.png

    Ligand Summary

    Reviews

    References

     

    No references found.

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    Files (2)

    FileSizeDateAttached by 
     2nyu-fr15172a.png
    2nyu vs fr15172a
    418.88 kB19:38, 22 Jul 2009qxuActions
     FR15172a-dimer.png
    FR15172A dimer
    175.74 kB19:28, 22 Jul 2009qxuActions
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