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BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM

NIAID Data Ecosystem2026-05-01 收录

酶催化机理

金属蛋白-气体相互作用

数据链接：

https://www.rcsb.org/structure/1C4C 数据链接链接失效反馈

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资源简介：

BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM

应用场景：

创建时间：

2023-08-09

配合物热力学

酶催化机理

The mono-μ-hydroxo complex {[Cu(tmpa)]2-(μ-OH)}3+ (1) can undergo reversible deprotonation at −30 °C to yield {[Cu(tmpa)]2-(μ-O)}2+ (2). This species is basic with a pKa of 24.3. 2 is competent for

NIAID Data Ecosystem90

CATALYTIC RNA ENZYME-PRODUCT COMPLEX

核酸酶结构

酶催化机理

CATALYTIC RNA ENZYME-PRODUCT COMPLEX Descriptor: CADMIUM ION, FIRST RNA FRAGMENT OF CLEAVED SUBSTRATE, RNA RIBOZYME STRAND, ... Authors: Murray, J.B, Szoke, H, Szoke, A, Scott, W.G. Deposit date: 2000

Protein Data Bank Japan2023-12-27 更新80

Crystal Structure of the P107C-MauG/pre-Methylamine Dehydrogenase Complex

蛋白质晶体

酶催化机理

Crystal Structure of the P107C-MauG/pre-Methylamine Dehydrogenase Complex Descriptor: 1,2-ETHANEDIOL, ACETATE ION, CALCIUM ION, ... Authors: Yukl, E.T, Wilmot, C.M. Deposit date: 2011-06-24 Release da

Protein Data Bank Japan2024-10-30 更新60

Models of the [FeFe]-hydrogenase active site: high symmetry in a biologically-relevant system

酶催化机理

化学模拟

The [FeFe]-hydrogenase enzymes are some of the best catalysts know for generating hydrogen. We have an ongoing programme to understand how their chemistry works, and to replicate the core 'active site

DataCite Commons2025-07-09 更新80

Crystal Structure of the Aminopeptidase from Vibrio proteolyticus in Complexation with Leucyl-leucyl-leucine.

蛋白质晶体

酶催化机理

Crystal Structure of the Aminopeptidase from Vibrio proteolyticus in Complexation with Leucyl-leucyl-leucine. Descriptor: Bacterial leucyl aminopeptidase, Peptide, (Leucyl-leucyl-leucine), ... Authors

Protein Data Bank Japan2024-11-20 更新60

BINDING OF EXOGENOUSLY ADDED CARBON MONOXIDE AT THE ACTIVE SITE OF THE FE-ONLY HYDROGENASE (CPI) FROM CLOSTRIDIUM PASTEURIANUM

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