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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 2.3.2.61.6 A resolution crystal structure
Display the word mapDisplay the reaction diagram Show all sequences 2.3.2.6crystal structures of the Escherichia coli LF-transferase complex with phenyalanyl adenosine (rA-Phe), with or without a short peptide bearing an N-terminal Arg residue. In the presence of both the donor and acceptor substrates, the peptide formation proceedes within the crystals, and the product peptide bearing Phe at the N terminus is retained on the LF-transferase
Display the word mapDisplay the reaction diagram Show all sequences 2.3.2.6enzyme adopts a monomeric structure consisting of two domains that form a bilobate molecule. The n-terminal domain forms a small lobe with an unusual fold. The large C-terminal domain has a highly conserved fold. Comparison with bacterial peptidoglycan synthase FemX
Display the word mapDisplay the reaction diagram Show all sequences 2.3.2.6in complex with minimal substrate phenylalanyl adenosine inhibitor puromycin
Display the word mapDisplay the reaction diagram Show all sequences 2.3.2.6in complex with puromycin. The p-methoxybenzyl group of puromycin is accomodated in a highly hydrophobic pocket. Model of complex with tRNA and a substrate bearing an N-terminal Arg or Lys
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