Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant Cysteine Protease Ervatamin B: Insight into the Structural Basis of its Stability and Substrate Specificity.

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Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant Cysteine Protease Ervatamin B: Insight into the Structural Basis of its Stability and Substrate Specificity. Descriptor: ERVATAMIN B, THIOSULFATE Authors: Chakrabarti, C, Biswas, S, Dattagupta, J.K. Deposit date: 2002-05-02 Release date: 2003-05-06 Last modified: 2024-11-20 Method: X-RAY DIFFRACTION (1.63 Å) Cite: Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: Some insights into the structural basis of its stability and substrate specificity Proteins, 51, 2003

植物半胱氨酸蛋白酶Ervatamin B的推定氨基酸序列与1.63埃X射线晶体结构：其稳定性与底物特异性的结构基础解析。描述符：Ervatamin B、硫代硫酸盐（THIOSULFATE）作者：Chakrabarti C、Biswas S、Dattagupta J.K. 提交日期：2002年5月2日发布日期：2003年5月6日最后修改日期：2024年11月20日实验方法：X射线衍射（X-RAY DIFFRACTION，分辨率1.63埃）引用文献：《植物半胱氨酸蛋白酶Ervatamin B的推定氨基酸序列与1.63埃X射线晶体结构：其稳定性与底物特异性的结构基础初探》，《Proteins》，第51卷，2003年

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2002-05-02