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X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE

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Protein Data Bank Japan2024-10-30 更新2026-03-21 收录
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https://pdbj.org/mine/summary/1bll
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X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE Descriptor: AMASTATIN, LEUCINE AMINOPEPTIDASE, ZINC ION Authors: Kim, H, Lipscomb, W.N. Deposit date: 1993-03-02 Release date: 1994-01-31 Last modified: 2024-10-30 Method: X-RAY DIFFRACTION (2.4 Å) Cite: X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state. Biochemistry, 32, 1993
创建时间:
1993-03-02
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