The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of protein of unknown function (NP_394501.1) from Thermoplasma acidophilum at 1.30 A resolution. To be published
    Site JCSG
    PDB Id 2re2 Target Id 376464
    Molecular Characteristics
    Source Thermoplasma acidophilum dsm 1728
    Alias Ids TPS1679,NP_394501.1, 336065 Molecular Weight 12492.53 Da.
    Residues 117 Isoelectric Point 5.80
    Sequence mkfavavsgdrvngpgeseevqiyetdggnvrliekysnpalnataargvfmlksaldhganalvlsei gspgfnfiknkmdvyivpempvadalklilegkvspatapthdhghhh
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.30 Rfree 0.179
    Matthews' coefficent 2.06 Rfactor 0.161
    Waters 336 Solvent Content 40.23

    Ligand Information


    Google Scholar output for 2re2
    1. NMR structure of the protein NP_247299. 1: comparison with the crystal structure
    K Jaudzems, M Geralt, P Serrano - Section F: Structural , 2010 - scripts.iucr.org
    2. Towards structure-based protein drug design
    C Zhang, L Lai - Biochemical Society Transactions, 2011 - www-06.all-portland.net

    Protein Summary


    Gene Ta1041m from Thermoplasma acidophilum encodes the NP_39401 protein from the NifX family (PF02579), which contains mostly iron-molybdenum cofactors (FeMo-co) involved in nitrogen fixation. Interestingly, the Thermoplasma acidophilum protein appears out of context,  is not a part of nif operon, but instead appears as a neighbor of a protein from DUF1288 family, a genomic context conserved in few other thermophilic bacteria.

    Literature references for the NifX family

    Rubio LM, Rangaraj P, Homer MJ, Roberts GP, Ludden PW; , J Biol Chem 2002;277:14299-14305.: Cloning and mutational analysis of the gamma gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster binding and protein stabilization. PUBMED:11823455

    Ligand Summary





    No references found.

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