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Q41714298-D25D8101-F0E0-4D24-B0EA-A31B1243447B
Q41714298-D25D8101-F0E0-4D24-B0EA-A31B1243447B
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http://www.wikidata.org/entity/statement/Q41714298-D25D8101-F0E0-4D24-B0EA-A31B1243447B
Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members.
P2860
Q41714298-D25D8101-F0E0-4D24-B0EA-A31B1243447B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41714298-D25D8101-F0E0-4D24-B0EA-A31B1243447B
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wasDerivedFrom
de457eb3db82ca79e3dc25388b4ae6641e4deb8e
P2860
Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function