Literature summary for 2.7.4.3 extracted from

Lu, Q.; Wang, J.
Single molecule conformational dynamics of adenylate kinase: energy landscape, structural correlations, and transition state ensembles (2008), J. Am. Chem. Soc., 130, 4772-4783.

Crystallization (Commentary)

Crystallization (Comment)	Organism
single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10°C to 50°C. Identification of key residues and contacts responsible for the conformational transitions are identified by following the time evolution of the two-dimensional spatial contact maps and characterizing the transition state as well as intermediate structure ensembles	Escherichia coli

Crystallization (Comment)

Organism

single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10°C to 50°C. Identification of key residues and contacts responsible for the conformational transitions are identified by following the time evolution of the two-dimensional spatial contact maps and characterizing the transition state as well as intermediate structure ensembles

Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	single molecule conformational dynamics for prediction of open and closed kinetic rates at the whole temperature ranges from 10°C to 50°C. Identification of key residues and contacts responsible for the conformational transitions are identified by following the time evolution of the two-dimensional spatial contact maps and characterizing the transition state as well as intermediate structure ensembles	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69441	-	-

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Release 2023.1 (January 2023)