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

    Title Crystal structure of putative hydrolase (2632844) from Bacillus subtilis at 1.96 A resolution. To be published
    Site JCSG
    PDB Id 2r11 Target Id 360559
    Molecular Characteristics
    Source Bacillus subtilis subsp. subtilis str. 168
    Alias Ids TPS1449,2632844 Molecular Weight 33308.02 Da.
    Residues 294 Isoelectric Point 5.81
    Sequence msnhsssipelsdngiryyqtyneslslwpvrcksfyistrfgqthviasgpedapplvllhgalfsst mwypniadwsskyrtyavdiigdknksipenvsgtrtdyanwlldvfdnlgiekshmiglslgglhtmn fllrmpervksaailspaetflpfhhdfykyalgltasngvetflnwmmndqnvlhpifvkqfkagvmw qdgsrnpnpnadgfpyvftdeelrsarvpillllgeheviydphsalhrassfvpdieaeviknaghvl smeqptyvnervmrffna
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 1.96 Rfree 0.239
    Matthews' coefficent 2.31 Rfactor 0.181
    Waters 985 Solvent Content 46.70

    Ligand Information


    Google Scholar output for 2r11
    1. Molecular Healing of Polymeric Materials, Coatings, Plastics, Elastomers, Composites, Laminates, Adhesives, and Sealants by Active Enzymes
    CS McDaniel, ME Wales, J Rawlins, P Cipi - US Patent App. 12/ , 2010 - Google Patents
    2. Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family
    S Montoro-Garca, I Martnez-Martnez - Journal of , 2009 - Am Soc Microbiol
    3. The unusual extended C-terminal helix of the peroxisomal [alpha]/[beta]-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization
    S Thoms, J Hofhuis, C Thing, J Grtner - Journal of structural , 2011 - Elsevier
    4. Enhancement of the enantioselectivity of carboxylesterase A by structure-based mutagenesis
    LF Godinho, CR Reis, HJ Rozeboom, FJ Dekker - Journal of , 2012 - Elsevier

    Protein Summary

    There are two highly homologous carboxylesterases in Bacillus subtilis 168. The CL4101A is CARBOXYLESTERASE NA which is 98% id from CARBOXYLESTERASE NP of Bacillus subtilis Thai I-8. The other YbfK is 64% identical to NP.  (Note: The sequence of NP in papers published by Quax's lab keeps changing, so maybe NP is actually the same as NA?).

    There is some literature in which NP is chemically characterized. It may be useful "Development of a new Bacillus carboxyl esterase for use in the resolution of chiral drugs". The structure itself isn't new fold, in fact, it is quite similar to many other enzymes in the pdb, mostly hydrolases. However, there are some differences around the active site, eg helix 207-220 of 1c4x is not present in CL4101A. The active site triad: S130-H274-D245. It is also interesting to see there are two conformers observed for the S130 (one is HB to H274, the other not).

    An N-terminal helix and a new dimerization mode are observed here for the first time within this fold.

    Ligand Summary





    No references found.

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