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The Open Protein Structure Annotation Network
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3rh7

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

    Title Crystal structure of a Hypothetical oxidoreductase (SMa0793) from SINORHIZOBIUM MELILOTI 1021 at 3.00 A resolution. To be published
    Site JCSG
    PDB Id 3rh7 Target Id 403543
    Molecular Characteristics
    Source Sinorhizobium meliloti 1021
    Alias Ids TPS30782,NP_435675.1, 2.30.110.10, 332672 Molecular Weight 33988.10 Da.
    Residues 320 Isoelectric Point 4.77
    Sequence madfqgetemtaevfdpralrdafgafatgvtvvtasdaagkpigftansftsvsldpplllvclakss rnyesmtsagrfainvlsetqkdvsntfarpvedrfaavdwrlgrdgcpifsdvaawfecsmqdiieag dhviiigrvtafensglnglgyarggyftprlagkavsaavegeirlgavleqqgavflagnetlslpn ctveggdpartlaayleqltglnvtigflysvyedksdgrqnivyhalasdgaprqgrflrpaelaaak fsssatadiinrfvlessignfgiyfgdetggtvhpiankdahs
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 6
    Resolution (Å) 3.00 Rfree 0.2265
    Matthews' coefficent 2.61 Rfactor 0.1867
    Waters Solvent Content 52.91

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    This sequence matches our family: Flavin_Reduct (PF01613). There are already many structures for this.

    Each chain is composed by two subdomains. The N-terminal has a FNM molecule bound and it folds into a FMN-binding split barrel. Sequece and structural analysis indicate that this region is a member of the Flavin reductase Pfam family (PF01613). FFAS, against Pfam, Flavin reductase like domain (PF01613.11, Score -77.100). Dali top hit: putative flavin reductase (2r0x-A, Z-score 24.4), that is a member of PF01613. No sequence motifs were idenfied for the C-terminal subdomain. Structural analysis using Dali indicated structural similarity with NUDIX HYDROLASE (3cng-A, Z-score 14.0) and PUTATIVE CTP PYROPHOSPHOHYDROLASE (3gwy-B, Z-score 13.2). Further, analysis should be performed to determine if this domain might have HYDROLASE activity)

    Ligand Summary

    Flavin mononucleotide (FMN). 

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    References

     

    No references found.

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