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The Open Protein Structure Annotation Network
PDB Keyword
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3cnh

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

    Title Crystal structure of predicted hydrolase of haloacid dehalogenase-like superfamily (NP_295428.1) from Deinococcus radiodurans at 1.66 A resolution. To be published
    Site JCSG
    PDB Id 3cnh Target Id 379311
    Molecular Characteristics
    Source Deinococcus radiodurans r1
    Alias Ids TPS1735,NP_295428.1, 87997 Molecular Weight 22712.68 Da.
    Residues 199 Isoelectric Point 4.99
    Sequence mtikalfwdiggvlltngwdreqradvaqrfgldtddfterhrlaapelelgrmtlaeyleqvvfyqpr dftpedfravmeeqsqprpevlalardlgqryrmyslnnegrdlneyrirtfglgefllafftssalgv mkpnpamyrlgltlaqvrpeeavmvddrlqnvqaaravgmhavqcvdaaqlreelaalgvr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.66 Rfree 0.187
    Matthews' coefficent 2.38 Rfactor 0.160
    Waters 344 Solvent Content 48.40

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The protein belongs to the the hydrolase family of proteins: PFAM PF00702 (http://www.sanger.ac.uk//cgi-bin/Pfam/getacc?PF00702). This family are structurally different from the alpha/ beta hydrolase family (Abhydrolase_1). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment. The rest of the fold is composed of the core alpha/beta domain.

    Figure 1: The core domain is on the left and the inserted helix bundle is on the right.

    The crystal structure is a dimer:

    Figure 2: Dimer structure.

    However, the protein's biological unit may be a tetramer:

    Figure 3: Biological unit predicted by PISA server.

    There are several structural homologs of the protein: 2gfh 2go7 2fea 2p11 2hx1 2hcf 2hsz 2hi0 2hdo 2pke 2g80 2ho4 2hf2 etc. Most of these are hydrolases.


    Ligand Summary

    NA and phosphate ions are modeled in each monomer. These ions may occupy the ligand binding site.

    References

    Reviews

    References

     

    No references found.

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