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Q34397043-C1BEB7FD-B88E-4E0C-BEE7-C882EE022F5D
Q34397043-C1BEB7FD-B88E-4E0C-BEE7-C882EE022F5D
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34397043-C1BEB7FD-B88E-4E0C-BEE7-C882EE022F5D
Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex
P2860
Q34397043-C1BEB7FD-B88E-4E0C-BEE7-C882EE022F5D
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34397043-C1BEB7FD-B88E-4E0C-BEE7-C882EE022F5D
rank
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type
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Statement
wasDerivedFrom
b43b5a96593124a558be7f4c58766f04c224ab78
P2860
Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex