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The Open Protein Structure Annotation Network
PDB Keyword
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1vm8

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Crystal structure of UDP-N-acetylglucosamine pyrophosphorylase (Agx2) from Mus musculus at 2.50 A resolution. To be published
    Site JCSG
    PDB Id 1vm8 Target Id 354660
    Molecular Characteristics
    Source Mus musculus
    Alias Ids TPS1338,16741099 Molecular Weight 58605.82 Da.
    Residues 522 Isoelectric Point 6.04
    Sequence mnvndlkqrlsqagqehllqfwnelseaqqvelymelqamnfeelnsffrkaigefdrsshqekvdarm epvprqvlgsatrdqeqlqaweseglsqisqnkvavlllaggqgtrlgvsypkgmydvglpshktlfqi qaerilklqqlaekhhgnkctipwyimtsgrtmestkefftkhkffglkkenvvffqqgmlpamsfdgk iileeknkvsmapdgngglyralaaqnivedmeqrgicsihvycvdnilvkvadprfigfciqkgadcg akvvektnptepvgvvcrvdgvyqvveyseislataqrrssdgrllfnagnianhfftvpflkdvvnvy epqlqhhvaqkkipyvdsqgyfikpdkpngikmekfvfdifqfakkfvvyevlredefsplknadsqng kdnpttarhalmslhhcwvlnagghfidengsrlpaiprsatngkseaitadvnhnlkdandvpiqcei splisyageglegyvadkefhapliidengvhelvkngi
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.50 Rfree 0.26573
    Matthews' coefficent 2.90 Rfactor 0.20676
    Waters 122 Solvent Content 57.25

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The gene 16741099 from  Mus musculus encodes an enzyme UDP-N-acetylglucosamine diphosphorylase (alternative names: N-acetylglucosamine-1-phosphate uridyltransferase, UDP-N-acetylglucosamine pyrophosphorylase) EC:2.7.7.23.  The enzyme catalyzes the nucleotidyl group transfer reaction: UTP + N-acetyl-alpha-D-glucosamine-1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine.  This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases) PF01704.  This enzyme is a part of UDP-N-acetylglucosamine biosynthesis pathway.  The protein belongs to the class of alpha and beta proteins (a+b) and reveals nucleotide-diphospho-sugar transferases fold type SCOP53447.  To date multiple structures of the enzyme homologues from different organisms have been determined: 1JV1, human; 2YQCCandida albicans.

    Ligand Summary



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