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                <attribute name="url">http://www.ebi.ac.uk/</attribute>
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        </source>
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                <names>
                    <shortLabel>lee-1996b-1</shortLabel>
                    <fullName>Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.</fullName>
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                            <shortLabel>in vitro</shortLabel>
                            <fullName>In vitro</fullName>
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                    </hostOrganism>
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                        <shortLabel>x-ray diffraction</shortLabel>
                        <fullName>x-ray crystallography</fullName>
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                <participantIdentificationMethod>
                    <names>
                        <shortLabel>predetermined</shortLabel>
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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="journal" nameAc="MI:0885">Biochemistry (0006-2960)</attribute>
                    <attribute name="publication year" nameAc="MI:0886">1996</attribute>
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        </experimentList>
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                    <shortLabel>f261_rat</shortLabel>
                    <fullName>6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1</fullName>
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                    <alias typeAc="MI:0301" type="gene name">Pfkfb1</alias>
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                        <fullName>Rattus norvegicus (Rat)</fullName>
                        <alias typeAc="MI:1041" type="synonym">Rat</alias>
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                    <shortLabel>pfkfb1-2</shortLabel>
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                            <shortLabel>N/A</shortLabel>
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                                        <end position="395"/>
                                        <isLink>false</isLink>
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                                </featureRangeList>
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                            <feature id="240884">
                                <names>
                                    <shortLabel>glu343</shortLabel>
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                                <featureType>
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                                        <shortLabel>binding region</shortLabel>
                                        <fullName>binding-associated region</fullName>
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                                </featureType>
                                <featureDetectionMethod>
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                                        <shortLabel>x-ray diffraction</shortLabel>
                                        <fullName>x-ray crystallography</fullName>
                                        <alias typeAc="MI:0303" type="go synonym">X-ray</alias>
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                                        <alias typeAc="MI:1041" type="synonym">X-ray</alias>
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                                    <shortLabel>his344</shortLabel>
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                                        <shortLabel>x-ray diffraction</shortLabel>
                                        <fullName>x-ray crystallography</fullName>
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                                        <alias typeAc="MI:1041" type="synonym">X-ray</alias>
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                                        <isLink>false</isLink>
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                            <feature id="240886">
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                                    <shortLabel>his349</shortLabel>
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                                    <primaryRef db="intact" dbAc="MI:0469" id="EBI-709914" refType="identity" refTypeAc="MI:0356"/>
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                                        <shortLabel>binding region</shortLabel>
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                                        <shortLabel>x-ray diffraction</shortLabel>
                                        <fullName>x-ray crystallography</fullName>
                                        <alias typeAc="MI:0303" type="go synonym">X-ray</alias>
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                                        <alias typeAc="MI:1041" type="synonym">X-ray</alias>
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                                                <shortLabel>certain</shortLabel>
                                                <fullName>certain sequence position</fullName>
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                                        <isLink>false</isLink>
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                                    <shortLabel>lys415</shortLabel>
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                                        <shortLabel>binding region</shortLabel>
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                                        <shortLabel>x-ray diffraction</shortLabel>
                                        <fullName>x-ray crystallography</fullName>
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                                        <alias typeAc="MI:1041" type="synonym">X-ray</alias>
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                                        <isLink>false</isLink>
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                            </feature>
                        </featureList>
                        <hostOrganismList>
                            <hostOrganism ncbiTaxId="83333">
                                <names>
                                    <shortLabel>ecoli</shortLabel>
                                    <fullName>Escherichia coli (strain K12)</fullName>
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                            </hostOrganism>
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                        <shortLabel>direct interaction</shortLabel>
                        <fullName>direct interaction</fullName>
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                <modelled>false</modelled>
                <intraMolecular>false</intraMolecular>
                <negative>false</negative>
                <attributeList>
                    <attribute name="3d-r-factors" nameAc="MI:0631">working 21.8%, free 27.8%</attribute>
                    <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>
