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Crystal structure of Cysteine peptidase (NP_982244.1) from BACILLUS CEREUS ATCC 10987 at 2.50 A resolution

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Protein Data Bank Japan2024-11-20 更新2026-03-21 收录
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Crystal structure of Cysteine peptidase (NP_982244.1) from BACILLUS CEREUS ATCC 10987 at 2.50 A resolution Descriptor: CHLORIDE ION, Cysteine peptidase, LYSINE Authors: Joint Center for Structural Genomics (JCSG) Deposit date: 2009-11-30 Release date: 2009-12-15 Last modified: 2024-11-20 Method: X-RAY DIFFRACTION (2.5 Å) Cite: Structural Analysis of Papain-Like NlpC/P60 Superfamily Enzymes with a Circularly Permuted Topology Reveals Potential Lipid Binding Sites. Plos One, 6, 2011

分辨率为2.50 Å的蜡样芽孢杆菌ATCC 10987(BACILLUS CEREUS ATCC 10987)半胱氨酸肽酶(Cysteine peptidase,NP_982244.1)的晶体结构 结构描述项:氯离子、半胱氨酸肽酶、赖氨酸 作者:联合结构基因组学中心(Joint Center for Structural Genomics, JCSG) 提交日期:2009-11-30 发布日期:2009-12-15 最后修改日期:2024-11-20 实验方法:X射线衍射(X-RAY DIFFRACTION,2.5 Å) 引用文献:《具有环状排列拓扑结构的木瓜蛋白酶样NlpC/P60超家族酶的结构分析揭示潜在脂质结合位点》,《公共科学图书馆·综合》(PLOS ONE),2011年,第6卷
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2009-11-30
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