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        <shortLabel>IntAct</shortLabel>
        <fullName>European Bioinformatics Institute</fullName>
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        <attribute name="url" nameAc="MI:0614">http://www.ebi.ac.uk/</attribute>
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        <attribute name="definition">INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions.</attribute>
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        <attribute name="postaladdress">European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom</attribute>
        <attribute name="url" nameAc="MI:0614">http://www.ebi.ac.uk/intact/</attribute>
      </attributeList>
    </source>
    <experimentList>
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        <names>
          <fullName>Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.</fullName>
        </names>
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          <attributeList>
            <attribute name="publication title" nameAc="MI:1091">Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.</attribute>
            <attribute name="journal" nameAc="MI:0885">Biochemistry (0006-2960)</attribute>
            <attribute name="publication year" nameAc="MI:0886">1996</attribute>
            <attribute name="author-list" nameAc="MI:0636">Lee YH., Ogata C., Pflugrath JW., Levitt DG., Sarma R., Banaszak LJ., Pilkis SJ.</attribute>
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            <names>
              <shortLabel>in vitro</shortLabel>
              <fullName>In vitro</fullName>
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          </hostOrganism>
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        <interactionDetectionMethod>
          <names>
            <shortLabel>x-ray diffraction</shortLabel>
            <fullName>x-ray crystallography</fullName>
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            <alias type="synonym" typeAc="MI:1041">x-ray diffraction</alias>
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        </interactionDetectionMethod>
        <participantIdentificationMethod>
          <names>
            <shortLabel>predetermined</shortLabel>
            <fullName>predetermined participant</fullName>
            <alias type="synonym" typeAc="MI:1041">predetermined</alias>
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          <xref>
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        <attributeList>
          <attribute name="author-list" nameAc="MI:0636">Lee YH., Ogata C., Pflugrath JW., Levitt DG., Sarma R., Banaszak LJ., Pilkis SJ.</attribute>
          <attribute name="accepted">Annotation to indicate that this entry has been checked and accepted by a senior curator.</attribute>
          <attribute name="journal" nameAc="MI:0885">Biochemistry (0006-2960)</attribute>
          <attribute name="publication year" nameAc="MI:0886">1996</attribute>
        </attributeList>
      </experimentDescription>
    </experimentList>
    <interactorList>
      <interactor id="2">
        <names>
          <shortLabel>f261_rat</shortLabel>
          <fullName>6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1</fullName>
          <alias type="gene name synonym" typeAc="MI:0302">6PF-2-K/Fru-2,6-P2ase liver isozyme</alias>
          <alias type="gene name" typeAc="MI:0301">Pfkfb1</alias>
        </names>
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          <secondaryRef db="rgd" dbAc="MI:0483" id="3307"/>
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            <fullName>protein</fullName>
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        </interactorType>
        <organism ncbiTaxId="10116">
          <names>
            <shortLabel>rat</shortLabel>
            <fullName>Rattus norvegicus (Rat)</fullName>
            <alias type="synonym" typeAc="MI:1041">Rat</alias>
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        </organism>
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        <attributeList>
          <attribute name="crc64">E307AF13945E0FCD</attribute>
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      </interactor>
    </interactorList>
    <interactionList>
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          <shortLabel>pfkfb1-2</shortLabel>
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        <participantList>
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            <interactorRef>2</interactorRef>
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                <shortLabel>unspecified role</shortLabel>
                <fullName>unspecified role</fullName>
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                  <fullName>neutral component</fullName>
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                  <shortLabel>glu339</shortLabel>
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                  <fullName>Escherichia coli (strain K12)</fullName>
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          <attribute name="3d-resolution" nameAc="MI:0632">2.00�</attribute>
          <attribute name="3d-structure" nameAc="MI:0630">The fructose-2,6-bisphosphatase domain has a core alpha/beta structure which consists of six stacked beta-strands, four parallel and two antiparallel. The core beta-sheet is surrounded by nine alpha-helices. The catalytic site, as defined by a bound phosphate ion, is positioned near the C-terminal end of the beta-sheet and close to the N-terminal end of an alpha-helix. The active site pocket is funnel-shaped.</attribute>
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</entrySet>