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2hq9

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

    Title Crystal structure of hypothetical protein (NP_107146.1) from MESORHIZOBIUM LOTI at 1.95 A resolution. To be published
    Site JCSG
    PDB Id 2hq9 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1505,NP_107146.1, 2.30.110.10, 90912
    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 2.19 Rfactor 0.18
    Waters
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    Solvent Content 43.33

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2hq9
    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. The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding property
    E Hilario, Y Li, D Niks, L Fan - Acta Crystallographica Section D: , 2012 - scripts.iucr.org
     

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    Protein Summary

    The gene mll6688 (NP_107146) of M. loti belongs to COG3467 (predicted flavin-nucleotide-binding proteins) and the pyridoxamine 5'-phosphate oxidase group (PF01243). The NP_107146 protein is predicted to have functional associations with NIFE_RHILO (nitrogenase iron-molybdenum cofactor biosynthesis protein nifE),  Q98AP6 (nitrogenase molybdenum-iron protein alpha chain, NifD), Q98AP5 (nitrogenase molybdenum-iron protein beta chain, NifK),  NIFN_RHILO (nitrogenase iron-molybdenum cofactor biosynthesis protein nifN), Q98K94 (hypothetical protein mll1578), Q98HQ7 (hypothetical protein mlr2758 ) and Q98P25 (hypothetical protein mlr9641).

    SCOP classifies the 3D structure of NP_107146 (2hq9) in the all beta class, FMN-binding split barrel fold, PNP oxidase-like family. 2hq9 is similar to proteins such as for example: BH0577 (PDB: 2hti-A; DALI Z-score 14.9; RMSD 2.4; 24% sequence identity within 117 superimposed residues), hypothetical protein (PDB: 2arz-A; DALI Z-score 14.8; RMSD 2.3; 13% sequence identity within 118 superimposed residues), hypothetical protein (PDB: 2iab-A; DALI Z-score 13.9; RMSD 2.6; 19% sequence identity within 118 superimposed residues).

    Analysis of the crystallographic packing of 2hq9 using the PQS server {Henrick, 1998 #73} indicates that a dimer is the likely biologically relevant form. A molecule of bound FAD per chain is observed in the crystal structure.

    Ligand Summary

    There are 18 residues interacting with FAD, but the most conserved are Pro35
    Tyr32, and Trp77 (Trp77 is from the opposite chain).

    References

    Reviews

    References

     

    No references found.

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