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3oox

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

    Title Crystal structure of a putative 2OG-Fe(II) oxygenase family protein (CC_0200) from CAULOBACTER CRESCENTUS at 1.44 A resolution. To be published
    Site JCSG
    PDB Id 3oox Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS29626,NP_419019.1, _0052.002434_, _0076.002207_, 327951
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.37 Rfactor 0.1690
    Waters
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    Solvent Content 48.10

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3oox
    1. Blind prediction of quaternary structures of homo-oligomeric proteins from amino acid sequences based on templates
    M Morita, M Kakuta, K Shimizu, S Nakamura - 2012 - hoajonline.com
     

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    Protein Summary

     Pfam Update: this protein is now in family: 2OG-FeII_Oxy (PF03171), which has many structures.

     

    Gene  NP_419019.1 from bacteria Caulobacter crescentus  ecodes the corresponding protein with 311 residues. The structure is characterized against MAD data with the resolution up to 1.70 Ang.  Sequence alignment indicates that this protein could be 2OG-Fe(II) oxygenase. Dali search and SSM alignment also suggest that this protein should be a structural homolog to 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme, isopenicillin N-synthase and deacetoxycephalosporin C-synthase.  The biolomolecule of protein NP_419019.1 should be a monomer according the interface interaction (PISA).

    398027_1.png

    Figure 1. Protein NP_419019.1 monomer.

    Ligand Summary

    Reviews

    References

     

    No references found.

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    315.58 kB18:04, 14 Jun 2010kevinjinActions
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