The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of a putative lipase (lip1) from Acinetobacter baumannii AYE at 1.70 A resolution. To be published
    Site JCSG
    PDB Id 4opm Target Id 420351
    Molecular Characteristics
    Source Acinetobacter baumannii aye
    Alias Ids TPS83372,YP_001714613.1 Molecular Weight 34048.37 Da.
    Residues 305 Isoelectric Point 8.01
    Sequence adnidvsfqtilqqernwaglqskslkvgditwsyseggsstkptlllihglagsrdnwnrvahylttn yhviipdlpgsgetivsqdfdysvpnlaeklrrfveaanlkgpihiaghslggsiallyagqypfetks lflvdsggifrsantiylkdptylkqllvskkgdfnyllkqtmfnppfipkeflqaqeklminqapqtq klvdqlialnkvytpdsfavltktidaptlilwgkqdkiinvevanelkrllknaqppvilenvghmpi leaeqlviqqyvpfllkvetnqssktttp
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.70 Rfree 0.1846
    Matthews' coefficent 2.69 Rfactor 0.1606
    Waters 701 Solvent Content 54.28

    Ligand Information



    Protein Summary

    This protein is a putative lipase. The structure has a potential active site triad Ser144, His298 and Asp269. The active site is also occupied by a PEG molecule, which likely functions as an analogue of the substrate.


    Most notably, this protein shows homology to human monoacylglycerol lipase ABHD6 (e.g. see ref Savinainen et al 2012; and Navia-Paldanius et al 2012), thus providing first structural homolog of the human protein.


    Fig. 1. PEG in spheres, active site triad shown as sticks


    Ligand Summary




    No references found.

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