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Structure of aminotransferase ilvE2 from Sinorhizobium meliloti complexed with PLP

NIAID Data Ecosystem2026-04-30 收录

支链氨基转移酶

蛋白质-辅因子相互作用

数据链接：

https://www.rcsb.org/structure/4JXU 数据链接链接失效反馈

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资源简介：

Structure of aminotransferase ilvE2 from Sinorhizobium meliloti complexed with PLP

应用场景：

创建时间：

2022-04-13

蛋白质-辅因子相互作用

代谢酶学

FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins

NIAID Data Ecosystem30

Protein∶co-factor and protein tetramerization contacts.

蛋白质-辅因子相互作用

蛋白质四聚化分析

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 pyrrole naming within the heme protoporphyrin ring). Atoms O1

Figshare2015-12-02 更新10

Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate

蛋白质晶体学

支链氨基转移酶

Crystal structure of oxidized human cytosolic branched-chain aminotransferase complexed with 4-methylvalerate Descriptor: 4-METHYL VALERIC ACID, MAGNESIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... Authors: Got

Protein Data Bank Japan2021-11-10 更新10

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

Apoflavodoxin/FMN binding energetics.

蛋白质-辅因子相互作用

热力学分析

Apoflavodoxin/FMN binding energetics.

Figshare2016-09-21 更新10