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Q27333834-22FA32E6-1BDF-4CAD-BE32-DFF432A71232
Q27333834-22FA32E6-1BDF-4CAD-BE32-DFF432A71232
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27333834-22FA32E6-1BDF-4CAD-BE32-DFF432A71232
Crystal Structure of OXA-58 with the Substrate-Binding Cleft in a Closed State: Insights into the Mobility and Stability of the OXA-58 Structure
P2860
Q27333834-22FA32E6-1BDF-4CAD-BE32-DFF432A71232
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27333834-22FA32E6-1BDF-4CAD-BE32-DFF432A71232
rank
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wasDerivedFrom
94240f21d1b21fb3d367756841be0ff93fddf704
P2860
Site-saturation mutagenesis of position V117 in OXA-1 β-lactamase: effect of side chain polarity on enzyme carboxylation and substrate turnover.