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            <date>2023-11-15</date>
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        <sites>
            <deposition>PDBe</deposition>
            <last_processing>PDBe</last_processing>
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        <key_dates>
            <deposition>2019-12-16</deposition>
            <header_release>2020-06-03</header_release>
            <map_release>2020-06-03</map_release>
            <update>2023-11-15</update>
        </key_dates>
        <grant_support>
            <grant_reference>
                <funding_body>European Research Council (ERC)</funding_body>
                <code>TransfoPneumo</code>
                <country>European Union</country>
            </grant_reference>
        </grant_support>
        <title>Escherichia coli AdhE structure in its compact conformation</title>
        <authors_list>
            <author>Fronzes R</author>
            <author>Pony P</author>
        </authors_list>
        <keywords>bacterial metabolism, OXIDOREDUCTASE</keywords>
    </admin>
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        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author ORCID="0000-0002-9740-8920" order="1">Pony P</author>
                    <author order="2">Rapisarda C</author>
                    <author ORCID="0000-0003-4279-9167" order="3">Terradot L</author>
                    <author ORCID="0000-0002-4820-3873" order="4">Marza E</author>
                    <author ORCID="0000-0003-3031-9824" order="5">Fronzes R</author>
                    <title>Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.</title>
                    <journal_abbreviation>Nat Commun</journal_abbreviation>
                    <country>UK</country>
                    <volume>11</volume>
                    <first_page>1426</first_page>
                    <last_page>1426</last_page>
                    <year>2020</year>
                    <external_references type="PUBMED">32188856</external_references>
                    <external_references type="DOI">doi:10.1038/s41467-020-15214-y</external_references>
                    <external_references type="ISSN">2041-1723</external_references>
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        <name>AdhE dimer in complex with NADH and Fe2+</name>
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                    <organism ncbi="83333">Escherichia coli (strain K12)</organism>
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                    <organism ncbi="83333">Escherichia coli K-12</organism>
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                <molecular_weight>
                    <theoretical units="MDa">0.09624411699999999</theoretical>
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                <number_of_copies>4</number_of_copies>
                <recombinant_expression database="NCBI">
                    <recombinant_organism ncbi="562">Escherichia coli</recombinant_organism>
                </recombinant_expression>
                <enantiomer>LEVO</enantiomer>
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KDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAA
GAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTF
DNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILI
GEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLVAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPA
SQGGIGDLYNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHK
RALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYE
HPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVM
DMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLG
VCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIADHLGLSAPGDRTAAKIEKLLA
WLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAP
AKAEKKAKKSA</string>
                    <external_references type="UNIPROTKB">P0A9Q7</external_references>
                </sequence>
                <ec_number>1.1.1.1</ec_number>
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                <molecular_weight>
                    <theoretical units="MDa">5.5845e-05</theoretical>
                </molecular_weight>
                <number_of_copies>2</number_of_copies>
                <formula>FE</formula>
            </ligand>
            <ligand macromolecule_id="3">
                <name>1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE</name>
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                    <theoretical units="MDa">0.000665441</theoretical>
                </molecular_weight>
                <number_of_copies>2</number_of_copies>
                <formula>NAI</formula>
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