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The Open Protein Structure Annotation Network
PDB Keyword
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2ou6

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

    Title Crystal structure of hypothetical protein (NP_294789.1) from Deinococcus radiodurans at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 2ou6 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1561,NP_294789.1, PF04978, 91359
    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 2.87 Rfactor 0.155
    Waters
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    Solvent Content 57.19

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2ou6
    1. 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
     
    2. Ligands in PSI structures
    A Kumar, HJ Chiu, HL Axelrod, A Morse - Section F: Structural , 2010 - scripts.iucr.org
     
    3. The structure of DinB from Geobacillus stearothermophilus: a representative of a unique four-helix-bundle superfamily
    DR Cooper, K Grelewska, CY Kim - Section F: Structural , 2010 - scripts.iucr.org
     

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    Protein Summary

    Gene DR_1065 from Deinococcus radiodurans encodes the NP_294789 protein that belongs to the DinB clan, DUF664 family (PF04978). SCOP classifies 2ou6 in the all alpha class, DinB/YfiT-like putative metalloenzymes, DinB-like family. Dali top hits for 2ou6 are with 2qnl (Z-scr=14), 2p1a (Z-scr=13) and the YfiT protein 1rxq (Z-scr=13).

     

    2ou6 coordinates a nickel ion using a triad of residues: H76, D168 and H172. However unlike most members of the superfamily that use three histidines this protein has an aspartate replacing the second histidine. The superfamily contains many members that have an aspartate or glutamate at this position and based on this structure we would expect that these are functional homologues rather than inactivated relatives.
     

    Ligand Summary


    References

    Reviews

    References

     

    No references found.

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