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The Open Protein Structure Annotation Network
PDB Keyword
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2gb3

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

    Title Crystal structure of Aspartate aminotransferase (tm1698) from Thermotoga maritima at 2.50 A resolution. To be published
    Site JCSG
    PDB Id 2gb3 Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1310,TM1698, 3.40.640.10
    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 6
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.02 Rfactor 0.229
    Waters
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    Solvent Content 39.03

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2gb3
    1. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
     
    2. Autoindexing the diffraction patterns from crystals with a pseudotranslation
    NK Sauter, PH Zwart - Acta Crystallographica Section D: Biological , 2009 - scripts.iucr.org
     
    3. Microbial drug target identification using different computational approaches: Specific application to Pseudomonas aeruginosa
    D Perumal, CS Lim - Innovations in Information , 2008 - ieeexplore.ieee.org
     

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    Protein Summary

    The gene TM1698 from Thermotoga maritima encodes the enzyme aspartate aminotransferase (AAT) from class I (fold I) family of pyridoxal phosphate (PLP)-dependent aspartate amino transferases PF00155 COG0075.  The protein belongs to the class of alpha and beta (a+b) proteins and reveals PLP-dependent transferase (a/b/a, mixed beta-sheet of 7 strands) fold type SCOP53382.  The enzyme is involved in amino acid biosynthesis.  The PLP cofactor is covalently attached to a conserved lysine residue through Schiff base linkage, forming aldimine intermediate.  The aldimine intermediate, depending on the reaction, is the substrate in four kinds of reactions: (1) transamination, (2) racemization, (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved.  The primary structure of the eukaryotic-type enzymes is quite well conserved, whereas the prokaryotic-type AAT is highly divergent (15% of identity) .

    Ligand Summary



    References

    Reviews

    References

     

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