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-Structure paper
タイトル | Role of remote scaffolding residues in the inhibitory loop pre-organization, flexibility, rigidification and enzyme inhibition of serine protease inhibitors |
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ジャーナル・号・ページ | Biochim. Biophys. Acta, Vol. 1824, Page 882-890, Year 2012 |
掲載日 | 2009年6月29日 (構造データの登録日) |
![]() | Majumder, S. / Khamrui, S. / Dasgupta, J. / Dattagupta, J.K. / Sen, U. |
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手法 | X線回折 |
解像度 | 2.25 - 2.97 Å |
構造データ | ![]() PDB-3i29: ![]() PDB-3qyd: ![]() PDB-3veq: |
化合物 | ![]() ChemComp-CA: ![]() ChemComp-HOH: |
由来 |
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![]() | HYDROLASE/HYDROLASE INHIBITOR / P1 and P2 MUTANT / TRYPSIN INHIBITOR / BOVINE TRYPSIN / COMPLEX / DIGESTION / HYDROLASE / METAL-BINDING / PROTEASE / SECRETED / SERINE PROTEASE / ZYMOGEN / PROTEASE INHIBITOR / SERINE PROTEASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX / Disulfide bond / HYDROLASE INHIBITOR / recombinant protein / mutant / chimeric protein beta barrel fold |