The Open Protein Structure Annotation Network
PDB Keyword


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

    Title Crystal structure of acetyltransferase of GNAT family (NP_373092.1) from STAPHYLOCOCCUS AUREUS MU50 at 2.20 A resolution. To be published
    Site JCSG
    PDB Id 3d8p Target Id 379875
    Molecular Characteristics
    Source Staphylococcus aureus subsp. aureus mu50
    Alias Ids TPS1749,NP_373092.1, 89059 Molecular Weight 19054.80 Da.
    Residues 162 Isoelectric Point 7.75
    Sequence mainiieynrsykeeliefilsiqknefnikidrddqpdleniehnylnsggqfwlainnhqnivgtig lirldnnmsalkkmfvdkgyrnlkigkklldkvimtckeqnidgiylgtidkfisaqyfysnngfreik rgdlpssfpkldvdnrfyyrnlkd
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.20 Rfree 0.218
    Matthews' coefficent 3.08 Rfactor 0.172
    Waters 228 Solvent Content 60.06

    Ligand Information


    Google Scholar output for 3d8p

    Protein Summary

    Acetyltransferase of GNAT family, where Tyr129 (corresponds to Tyr141 in PDB:1tiq) is predicted as the catalytic residue. NP_373092.1 is from Staphylococcus aureus mu50.  Based on sequence alignment from NCBI blast and the predicted homologues Fold & Function Assignment System (FFAS and SSM), this target is structurally similar to 1TIQ, 1YR0, 2OB0, 2PSW and 2Q7B, which are acetyltransferase protein most likely.  Both SEC data and interaction interface calculation suggest the biomolecule of NP_373092.1 is a monomer.




    Figure 1. Biomolecule of protein NP_373092.1 should be a monomer. 



    Figure 2. Protein NP_373092.1(Green) is a structural homolog to those acetyltransferase, such as 1TIQ, 1YR0, 2OB0, 2PSW and 2Q7B.

    Ligand Summary

    Ca2+, Acetate ions


    Forouhar, F.,  Lee, I.S.,  Vujcic, J.,  Vujcic, S.,  Shen, J.,  Vorobiev, S.M.,  Xiao, R.,  Acton, T.B.,  Montelione, G.T.,  Porter, C.W.,  Tong, L.  (2005) Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.  J.Biol.Chem.  280: 40328-40336 




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