The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of histidinol-phosphate aminotransferase (YP_297314.1) from RALSTONIA EUTROPHA JMP134 at 2.05 A resolution. To be published
    Site JCSG
    PDB Id 3euc Target Id 391227
    Molecular Characteristics
    Source Ralstonia eutropha jmp134
    Alias Ids TPS18340,YP_297314.1, 3.40.640.10, 87424 Molecular Weight 39604.61 Da.
    Residues 366 Isoelectric Point 5.50
    Sequence msvvdpslieriirddvramgayhvpdshglvkldamenpyrlppalrselaarlgevalnrypvpsse alraklkevmqvpagmevllgngsdeiismlalaaarpgakvmapvpgfvmyamsaqfaglefvgvplr adftldrgamlaamaehqpaivylaypnnptgnlfdaadmeaivraaqgsvcrslvvvdeayqpfaqes wmsrltdfgnllvmrtvsklglagirlgyvagdpqwleqldkvrppynvnvlteatalfalehvavlde qaaqlraersrvaegmaahggvtvfpsaanfllarvpdaaqtfdrllarkvliknvskmhpllanclrv tvstpeenaqfleafaaslqd
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.05 Rfree 0.237
    Matthews' coefficent 2.46 Rfactor 0.194
    Waters 381 Solvent Content 50.03

    Ligand Information


    Google Scholar output for 3euc

    Protein Summary

    That target YP_297314.1 is Histidinol-phosphate aminotransferase enzyme from Ralstonia eutropha JMP134. It belongs to PFAM PF00155.


    The monomer structure can be devided into two domains: one with a seven tranded sheet surrounded by helices and the other with two stranded sheet surrounded by helices, as shown below.


    The protein, however, occurs as a dimer in crystallographic asu, and this may represent its oligomeric organization in solution.



    The two chains of the protein differ slightly in conformation at the N-terminus, shown below as the chain A is superimposed on chain B.



    There are a number of structural homologs of this protein as obtained from SSM search. Some of these are shown below superimposed on each other: 391227(green), 1fg3(cyan), 1fg7(magenta), 1gew(yellow), 1gey(pink), 1h1c(grey), 3cq4(blue), 3cq5(orange), 3cq6(pale cyan)


    Some of these homolgs have ligands bound in the active site, although, no ligand was observed in this structure.





    A sequence alignment of the proteins highlights the consderved residues (underlined by red carets), shown below.




    •        Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS; , Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477.: Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. PUBMED:10417420
    •       Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K; , Biochemistry 1999;38:2413-2424.: Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. PUBMED:10029535

    Ligand Summary




    No references found.

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