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Q27681138-73EA8C9D-EB51-4F9E-8B29-3E71A2CA97EF
Q27681138-73EA8C9D-EB51-4F9E-8B29-3E71A2CA97EF
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http://www.wikidata.org/entity/statement/Q27681138-73EA8C9D-EB51-4F9E-8B29-3E71A2CA97EF
Structure of the catalytic chain ofMethanococcus jannaschiiaspartate transcarbamoylase in a hexagonal crystal form: insights into the path of carbamoyl phosphate to the active site of the enzyme
P2860
Q27681138-73EA8C9D-EB51-4F9E-8B29-3E71A2CA97EF
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27681138-73EA8C9D-EB51-4F9E-8B29-3E71A2CA97EF
rank
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wasDerivedFrom
1e7271907856460243f3237b4114f5927a201e1b
P2860
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.