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The Open Protein Structure Annotation Network
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2hlj

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

    Title Crystal structure of hypothetical protein (NP_742468.1) from Pseudomonas putida KT2440 at 2.00 A resolution. To be published
    Site JCSG
    PDB Id 2hlj Target Id 366984
    Molecular Characteristics
    Source Pseudomonas putida kt2440
    Alias Ids TPS1494,NP_742468.1, 90894 Molecular Weight 17651.08 Da.
    Residues 156 Isoelectric Point 5.78
    Sequence mpalityrttvqedwvdynghlrdafyllifsyatdalmdrigldadsrgqsgnslftleahinylhev klgtevwvqtqilgfdrkrlhvyhslhragfdevlaaseqmllhvdlagpqsapfghttvcrlnhlveq qegaqapqymgrtiklpa
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.00 Rfree 0.227
    Matthews' coefficent 2.21 Rfactor 0.167
    Waters 170 Solvent Content 44.00

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2hlj
    1. Domain definition and target classification for CASP7
    ND Clarke, I Ezkurdia, J Kopp, RJ Read - Proteins: Structure, , 2007 - Wiley Online Library
     
    2. Analysis of proteins with the'hot dog'fold: Prediction of function and identification of catalytic residues of hypothetical proteins
    LS Pidugu, K Maity, K Ramaswamy - BMC structural , 2009 - biomedcentral.com
     
    3. Structure of the putative thioesterase protein TTHA1846 from Thermus thermophilus HB8 complexed with coenzyme A and a zinc ion
    T Hosaka, K Murayama, M Kato-Murayama - Section D: Biological , 2009 - scripts.iucr.org
     

    Protein Summary

    The gene KT2440 (NP_742468.1) from Pseudomonas putida encodes a putative 4-hydroxybenzoyl-CoA thioesterase (4HBT) EC:3.1.2.23, a member of thioesterase superfamily PF03061.  The enzyme belongs to the class of alpha and beta (a+b) proteins and adopts a thioesterase/thiol ester dehydrase-isomerase fold type SCOP54636.  The enzyme catalyzes the following reaction: 4-hydroxybenzoyl-CoA + H(2)O <=> 4-hydroxybenzoate + CoA.  This is the final step of the 4-chlorobenzoate degradation pathway.   The biological form of 4HBT is a homotetramer with four active sites.  Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).  Several structures of the enzyme homologues a from different Pseudomonas sp. strain have been solved: 1LO8 1LO7.

    Ligand Summary



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