1AIX
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![BU of 1aix by Molmil](/molmil-images/mine/1aix) | HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL | 分子名称: | ALPHA-THROMBIN (LARGE SUBUNIT), ALPHA-THROMBIN (SMALL SUBUNIT), HIRUGEN, ... | 著者 | Skordalakes, E, Dodson, G, Elgendy, S, Goodwin, C.A, Green, D, Tyrrel, R, Scully, M.F, Freyssinet, J, Kakkar, V.V, Deadman, J. | 登録日 | 1997-04-30 | 公開日 | 1997-10-15 | 最終更新日 | 2013-03-13 | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | 主引用文献 | The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci., 1, 1992
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1A3B
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![BU of 1a3b by Molmil](/molmil-images/mine/1a3b) | COMPLEX OF HUMAN ALPHA-THROMBIN WITH THE BIFUNCTIONAL BORONATE INHIBITOR BOROLOG1 | 分子名称: | ALPHA-THROMBIN (LARGE SUBUNIT), ALPHA-THROMBIN (SMALL SUBUNIT), Hirudin, ... | 著者 | Skordalakes, E, Elgendy, S, Dodson, G, Goodwin, C.A, Green, D, Scully, M.F, Freyssinet, J.H, Kakkar, V.V, Deadman, J. | 登録日 | 1998-01-20 | 公開日 | 1998-06-03 | 最終更新日 | 2011-07-13 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Bifunctional peptide boronate inhibitors of thrombin: crystallographic analysis of inhibition enhanced by linkage to an exosite 1 binding peptide. Biochemistry, 37, 1998
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1AI8
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![BU of 1ai8 by Molmil](/molmil-images/mine/1ai8) | HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH THE EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROMPG | 分子名称: | ALPHA-THROMBIN (LARGE SUBUNIT), ALPHA-THROMBIN (SMALL SUBUNIT), HIRUDIN IIIB, ... | 著者 | Skordalakes, E, Dodson, G, Elgendy, S, Goodwin, C.A, Green, D, Tyrrel, R, Scully, M.F, Freyssinet, J, Kakkar, V.V, Deadman, J. | 登録日 | 1997-05-01 | 公開日 | 1997-10-15 | 最終更新日 | 2023-08-02 | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | 主引用文献 | The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci., 1, 1992
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