Literature summary for 2.5.1.58 extracted from

Sousa, S.F.; Fernandes, P.A.; Ramos, M.J.
Molecular dynamics simulations on the critical states of the farnesyltransferase enzyme (2009), Bioorg. Med. Chem., 17, 3369-3378.

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations to study enzyme flexibility in the 4 key intermediate states formed during the FTase catalytic mechanisms, ie. FTase resting state, binary complex FTase-FPP, ternary complex FTase-FPP-peptide, and product complex FTase-product. Relatively small-scale events such as substrate binding or product formation cause minor changes at the neighboring residues and corresponding helices, but ultimately induce much more dramatic effects on the more external regions of the enzyme	Rattus norvegicus

Crystallization (Comment)

Organism

molecular dynamics simulations to study enzyme flexibility in the 4 key intermediate states formed during the FTase catalytic mechanisms, ie. FTase resting state, binary complex FTase-FPP, ternary complex FTase-FPP-peptide, and product complex FTase-product. Relatively small-scale events such as substrate binding or product formation cause minor changes at the neighboring residues and corresponding helices, but ultimately induce much more dramatic effects on the more external regions of the enzyme

Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

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Release 2023.1 (January 2023)