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The Open Protein Structure Annotation Network
PDB Keyword
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3bxp

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

    Title Crystal structure of putative carboxylesterase (NP_786266.1) from Lactobacillus plantarum at 1.70 A resolution. To be published
    Site JCSG
    PDB Id 3bxp Target Id 379483
    Molecular Characteristics
    Source Lactobacillus plantarum
    Alias Ids NP_786266.1 Molecular Weight 30416.98 Da.
    Residues 276 Isoelectric Point 6.33
    Sequence mqveqrtlntaahpfqitaywldqisdfetavdypimiicpgggftyhsgreeapiatrmmaagmhtvvl nyqlivgdqsvypwalqqlgatidwittqasahhvdcqriilagfsagghvvatyngvatqpelrtryh ldhyqgqhaaiilgypvidltagfpttsaarnqittdarlwaaqrlvtpaskpafvwqtatdesvppin slkyvqamlqhqvatayhlfgsgihglalanhvtqkpgkdkylndqaaiwpqlalrwlqeqgllagny
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.70 Rfree 0.197
    Matthews' coefficent 2.30 Rfactor 0.166
    Waters 383 Solvent Content 46.49

    Ligand Information
    Ligands EPE (4-(2-HYDROXYETHYL)-1-PIPERAZINE) x 2;PGR (R-1,2-PROPANEDIOL) x 3;PGO (S-1,2-PROPANEDIOL) x 4
    Metals CL (CHLORIDE) x 1

    Jmol

    Protein Summary

    The lp_2923 gene from Lactobacillus plantarum encodes a putative carboxylesterase from Lactobacillus plantarum.The protein shows sequence homology to members of Pfam PF07859 as determined by FFAS. Dali search results can find several similar structures such as 3BJR  (NP_784706.1), 1JKM, 2HU7, 1JFR. Based on interface interaction calculation, this target may be a dimer.

    lp_2923
    has been directly compared with 379491, which is also from Lactobacillus plantarum. Both structures adopt a similar ?/?-hydrolase fold. In the structure of NP_784706.1, the conserved catalytic triad, Ser 113, Asp197 and His229, can be identified easily via direct structural comparison with other homologs. The TCOFFEE alignment between 379483 and 379491 indicates that these two targets have an almost identical sequence. Correspondingly, Ser 116, Asp 201 and His 233 in 379483 should  be the conserved catalytic triad, as confirmed by direct structural comparison.

           

    Ligand Summary



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