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The Open Protein Structure Annotation Network
PDB Keyword
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2a3n

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

    Title Crystal structure of Putative glucosamine-fructose-6-phosphate aminotransferase (16423107) from SALMONELLA TYPHIMURIUM LT2 at 1.35 A resolution. To be published
    Site JCSG
    PDB Id 2a3n Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1398,16423107, 3.40.50.10490, 432394
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 1.83 Rfactor 0.112
    Waters
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    Solvent Content 32.40

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2a3n
    1. 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
     
    2. Probing the active site of the sugar isomerase domain from E. coli arabinose_5_phosphate isomerase via X_ray crystallography
    LJ Gourlay, S Sommaruga, M Nardini - Protein , 2010 - Wiley Online Library
     

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    Protein Summary

    The gene STM4540.S from Salmonella typhimurium lt2 encodes the NP_463399 protein, a glucosamine-fructose-6-phosphate aminotransferase (EC2.6.1.16) from the family of the class II aminotransferases, a superfamily of sugar isomerases containing a SIS domain (PF01380). The other names of this enzyme are glutamine-fructose-6-phosphate transaminase, D-fructose-6-phosphate amidotransferase, or GlcN6P synthase.  

    The 2a3n structure belongs to the class of alpha and beta proteins (a+b) and reveals a SIS domain fold type SCOP53696.  According to DALI, similar structures to 2a3n are: the Yurp protein

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    (Z=40), the putative isomerase
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    (Z=38, topsan-3fkj), the crystal structure of the human homologue
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    (Z=33) and
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    (Z=32).

    The enzyme is widely distributed in nature.  The enzyme catalyzes the reaction involving ammonia transfer and sugar phosphate isomerization:

    L-glutamine + D-fructose 6-phosphate -> D-glucosamine 6-phosphat + L-glutamate.

    The reaction mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a conserved lysine residue at the active site. This reaction is the first committed step of the cytoplasmic biosynthetic pathway leading to the formation of uridine 5'-diphospho-N-acetylglu-cosamine (UDP-GlcNAc). The final product of this pathway is an activated precursor of numerous macromolecules containing amino sugars, including chitin and mannoproteins in fungi, peptidoglycan and lipopolysaccharides in bacteria, and glycoproteins in mammals [Ref]

    Ligand Summary



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