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Streptavidin variant S112E-K121H bound to bis-biotinylated Iron-porphyrin

NIAID Data Ecosystem2026-05-10 收录

蛋白质-辅因子相互作用

生物传感器结构设计

数据链接：

https://www.rcsb.org/structure/8TY0 数据链接链接失效反馈

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资源简介：

Streptavidin variant S112E-K121H bound to bis-biotinylated Iron-porphyrin

应用场景：

创建时间：

2025-10-01

蛋白质-辅因子相互作用

甲基化组学

The aim of the project is to identify proteins the ustilize S-adenosyl methionine as cofactor for performing methylation of target molecules in D. melanogaster S2 cells. For this purpose, we applied a

NIAID Data Ecosystem60

Comparative analysis of interaction of cofactor (NADPH) with HCTR1 and HCTR2 before and after MD simulation.

蛋白质-辅因子相互作用

分子动力学模拟

Comparative analysis of interaction of cofactor (NADPH) with HCTR1 and HCTR2 before and after MD simulation.

NIAID Data Ecosystem20

NAD

蛋白质-辅因子相互作用

NADH构象分类

Background: -------------- Nicotinamide adenine dinucleotide (NADH) is a ubiquitous redox cofactor that participates in a wide range of enzymatic and regulatory processes. These include metabolism, si

Mendeley Data10

Protein∶co-factor and protein tetramerization contacts.

蛋白质-辅因子相互作用

蛋白质四聚化

aAtom CBB is the terminal vinyl methylene carbon of pyrrole ring b, and atom CMA is the methyl carbon of pyrrole ring a (see Figure 4D for

NIAID Data Ecosystem30

Woodward & Ikeya - Microspectroscopy of DmCRY-CT / FAD binding and aggregation (in Bradlaugh et al 2025).

蛋白质-辅因子相互作用

光调控蛋白质聚集动力学

Video of fluorescence microspectroscopy based in vitro characterisation of DmCRY-CT / FAD binding and aggregation. 100 μM DmCRY-CT solution with 10 μM FAD (pH 7.4) leads to emissive particle formation

NIAID Data Ecosystem20

Streptavidin variant S112E-K121H bound to bis-biotinylated Iron-porphyrin

资源简介：

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