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The Open Protein Structure Annotation Network
PDB Keyword
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3h3h

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

    Title Crystal structure of SnoaL-like protein of unknown function (YP_438428.1) from Burkholderia thailandensis E264 at 1.60 A resolution. To be published
    Site JCSG
    PDB Id 3h3h Target Id 390584
    Molecular Characteristics
    Source Burkholderia thailandensis e264
    Alias Ids TPS20852,YP_438428.1, 3.10.450.50, 325250 Molecular Weight 13635.80 Da.
    Residues 121 Isoelectric Point 6.03
    Sequence mepitqafaqqfsrewidawnahdldailshyadgfemsspmivqiagepsgrlrgkeqvgaywrealr mipdlhfewiatlagvdsvaihyrgakgrlalevfhfgpdrrvvkalahyag
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.60 Rfree 0.202
    Matthews' coefficent 1.98 Rfactor 0.179
    Waters 171 Solvent Content 37.81

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3h3h
    1. Ligands in PSI structures
    A Kumar, HJ Chiu, HL Axelrod, A Morse - Section F: Structural , 2010 - scripts.iucr.org
     

    Protein Summary

    Pfam note: this protein is now in family PF07366. 5 SnoaL in CL0051, with other structures.

     

     

     

    Gene BTH_II0226 from Burkholderia thailandensis encodes the YP_438428.1 protein that belongs to the SnoaL-like polyketide cyclase family (PF07366).  The BLAST search results indicate that this protein is a member of the NTF2-like  superfamily. 

    Pre-SCOP classifies 3h3h in the alpha+beta class, NTF2-like superfamily, ketosteroid isomerase-like (KIS) family. DALI, FFAS and SSM suggest that 3h3h is a structurally similar to ketosteroid isomerases and steroid delta-isomerases like PDB:1qjg, PDB:1ocv, PDB:8cho, PDB:3fzw (Z=16). However, the active site is very different to these structures. The ketosteroid isomerases have an active site formed by residues Tyr16, Tyr32, Asp40, Tyr57, and Asp103 (numbering from wild type KIS PDB entry PDB:1opy) which corresponds to residues Trp16, Tyr32, Ser40, Trp64, and Glu102. In fact, residues Trp16, Trp20, Tyr32, Met42, Trp64, Tyr92, Glu102, Tyr104 and Tyr119 sketch a very hydrophobic active site cavity in each subunit with unassigned electron density. One unknown ligand is modeled in each putative active site. The interface interaction indicates that the biomolecule of protein YP_438428.1 could be a dimer.

     

     

     

     

     

     

     

    Ligand Summary

    Unknown ligand

    Reviews

    References

     

    No references found.

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