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Q27664635-E74A6A1A-CBD3-47F7-93B8-D61C9109E851
Q27664635-E74A6A1A-CBD3-47F7-93B8-D61C9109E851
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27664635-E74A6A1A-CBD3-47F7-93B8-D61C9109E851
Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft
P2860
Q27664635-E74A6A1A-CBD3-47F7-93B8-D61C9109E851
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27664635-E74A6A1A-CBD3-47F7-93B8-D61C9109E851
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type
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wasDerivedFrom
08501a5ab37c0f2d3d9589edaf06ee613b41e33b
P2860
Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases