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2hcf

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

    Title Crystal structure of hydrolase haloacid dehalogenase-like family (np_662590.1) from Chlorobium tepidum TLS at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 2hcf Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1484,NP_662590.1, 104741
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.01 Rfactor 0.189
    Waters
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    Solvent Content 38.41

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2hcf
    1. Assessment of predictions submitted for the CASP7 function prediction category
    G Lopez, A Rojas, M Tress - : Structure, Function, and , 2007 - Wiley Online Library
     
    2. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    3. Domain definition and target classification for CASP7
    ND Clarke, I Ezkurdia, J Kopp, RJ Read - Proteins: Structure, , 2007 - Wiley Online Library
     
    4. Modeling the resting state of oxalate oxidase and oxalate decarboxylase enzymes
    M Scarpellini, J Gtjens, OJ Martin, JW Kampf - Inorganic , 2008 - ACS Publications
     

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    Protein Summary

    The gene NP_662590.1 from Chlorobium tepidum encodes a haloacid dehalogenase (HAD)-like hydrolase PF00702.  The enzyme belongs to the class of alpha and beta (a+b) proteins and adopts a HAD-like fold type SCOP56783. The HAD superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others, all of which use a nucleophilic aspartate in their phosphoryl transfer reaction. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable.  Several structures of the enzyme homologues from other organisms are available: 3KZXEhrlichia chaffeensis; 3KC2Saccharomyces cerevisiae.

    Ligand Summary



    References

    Reviews

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