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The Open Protein Structure Annotation Network
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1vl2

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

    Title Crystal structure of Argininosuccinate synthase (TM1780) from Thermotoga maritima at 1.65 A resolution. To be published
    Site JCSG
    PDB Id 1vl2 Target Id 283634
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1314,TM1780, 282261 Molecular Weight 46051.53 Da.
    Residues 409 Isoelectric Point 5.94
    Sequence mkekvvlaysggldtsvilkwlcekgfdviayvanvgqkddfvaikekalktgaskvyvedlrrefvtd yiftallgnamyegryllgtaiarpliakrqveiaekegaqyvahgatgkgndqvrfeltyaalnpnlk vispwkdpeflakfkgrtdlinyamekgipikvskkrpysedenlmhisheagkledpahipdedvftw tvspkdapdeetlleihfengipvkvvnlkdgtektdplelfeylnevgakngvgrldmvenrfigiks rgvyetpgatilwiahrdlegitmdkevmhlrdmlapkfaeliyngfwfspemefllaafrkaqenvtg kvtvsiykgnvmpvaryspyslynpelssmdveggfdatdskgfinihalrlkvhqlvkkgyqr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 1.65 Rfree 0.2094
    Matthews' coefficent 2.16 Rfactor 0.17742
    Waters 1184 Solvent Content 42.67

    Pathway

    Reactions found in Metabolic Reconstruction for TM1780

    Name: "argininosuccinate synthase, reversible"
    Metabolic Subsystem: Arginine Biosynthesis
    Reaction: : asp-L + atp + citr-L <==> amp + argsuc + h + ppi
    Classification: EC:6.3.4.5
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vl2
    1. Structure of human argininosuccinate synthetase
    T Karlberg, R Collins, S van den Berg - Section D: Biological , 2008 - scripts.iucr.org
     

    Protein Summary

    The gene TM1780 from Thermotoga maritima encodes argininosuccinate synthase PF00764 COG0137, a member of N-type ATP pyrophosphatases.  The protein belongs to the class of alpha and beta proteins (a+b) and reveals adenine nucleotide alpha hydrolase-like fold SCOP52373. The argininosuccinate synthase is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis, which is the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. The biological unit of the enzyme is homotetramer.  The sequences of this enzyme from various prokaryotes, archaebacteria and eukaryotes show significant similarity.  The crystal structure of human homologue is available 2NZ2.

    Ligand Summary



    References

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