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 N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from Thermotoga maritima at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 1vkn Target Id 283635
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1315,TM1782, 89512 Molecular Weight 37933.69 Da.
    Residues 339 Isoelectric Point 6.04
    Sequence miragiigatgytglelvrllknhpeakitylssrtyagkkleeifpstlensilsefdpekvskncdv lftalpagasydlvrelkgvkiidlgadfrfddpgvyrewygkelsgyenikrvyglpelhreeiknaq vvgnpgcyptsvilalapalkhnlvdpetilvdaksgvsgagrkekvdylfsevneslrpynvakhrhv pemeqelgkisgkkvnvvftphlvpmtrgilstiyvktdksleeiheaylefyknepfvhvlpmgiyps tkwcygsnhvfigmqmeertntlilmsaidnlvkgasgqavqnmnimfgldetkgleftpiyp
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 1.80 Rfree 0.21182
    Matthews' coefficent 2.28 Rfactor 0.17766
    Waters 756 Solvent Content 46.17


    Reactions found in Metabolic Reconstruction for TM1782

    Name: N-acetyl-g-glutamyl-phosphate reductase
    Metabolic Subsystem: Arginine Biosynthesis
    Reaction: : acg5sa + nadp + pi <==> acg5p + h + nadph
    Classification: EC:

    Ligand Information


    Google Scholar output for 1vkn
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
    2. 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
    3. On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination
    S Panjikar, V Parthasarathy, VS Lamzin - Section D: Biological , 2009 - scripts.iucr.org
    4. High throughput crystallography of TB drug targets
    AC Murillo, HY Li, T Alber, EN Baker - Current Drug Targets , 2007 - ingentaconnect.com
    5. Fitting molecular fragments into electron density
    K Cowtan - Acta Crystallographica Section D: Biological , 2007 - scripts.iucr.org
    6. High-throughput protein production for X-ray crystallography and use of size exclusion chromatography to validate or refute computational biological unit predictions
    D McMullan, JM Canaves, K Quijano - Journal of structural and , 2005 - Springer
    7. Crystal Structure of N-acetyl-_-glutamyl-phosphate Reductase from Mycobacterium tuberculosis in Complex with NADP+
    LT Cherney, MM Cherney, CR Garen, C Niu - Journal of molecular , 2007 - Elsevier
    8. Crystal structure of putative N_Acetyl___glutamyl_phosphate reductase (AK071544) from rice (Oryza sativa)
    T Nonaka, A Kita, J Miura_Ohnuma - Proteins: Structure, , 2005 - Wiley Online Library
    9. Expression, purification, crystallization and preliminary X-ray analysis of two arginine-biosynthetic enzymes from Mycobacterium tuberculosis
    F Moradian, C Garen, L Cherney - Section F: Structural , 2006 - scripts.iucr.org
    10. Improved expression, purification and crystallization of a putative N-acetyl--glutamyl-phosphate reductase from rice (Oryza sativa)
    J Miura-Ohnuma, T Nonaka, S Katoh - Section F: Structural , 2005 - scripts.iucr.org
    11. Molecular replacement: the probabilistic approach of the program REMO09 and its applications
    R Caliandro, B Carrozzini, GL Cascarano - A: Foundations of , 2009 - scripts.iucr.org
    12. Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and tetrapeptidic fragments
    F Pavelcik, J Vaclavik - Acta Crystallographica Section D: Biological , 2010 - scripts.iucr.org

    Protein Summary

    The gene TM1782 from Thermotoga maritima encodes the enzyme N-acetyl-gamma-glutamyl-phosphate reductase PF01118 COG0014. Alternative names: N-acetylglutamate 5-semialdehyde dehydrogenase, N-acetylglutamic gamma-semialdehyde dehydrogenase.  The enzyme belongs to the class of alpha and beta proteins and reveals NAD(P)-binding Rossmann-fold domain fold type SCOP51734.  The enzyme participates in urea cycle and metabolism of amino groups. 

    Ligand Summary





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