Literature summary for 3.4.21.4 extracted from

Blankenship, E.; Vukoti, K.; Miyagi, M.; Lodowski, D.T.
Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state (2014), Acta Crystallogr. Sect. D, 70, 833-840.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of unmodified, unliganded trypsin crystallized at physiological pH, to 0.81 A resolution. Comparisons of the catalytic triad confirm the conserved position of the catalytic residues in an unoccupied active site, and demonstrate great mobility of the catalytic serine. The two conformations of the catalytic serine show some conformational fluidity in the active site of unliganded trypsin. The hydrogen-bonding network between the residues of the catalytic triad and neighbouring bonding partners is seen in the majority of serine protease structures determined to date, implying that much of this network is maintained in the unliganded state	Saccharopolyspora erythraea

Crystallization (Comment)

Organism

structure of unmodified, unliganded trypsin crystallized at physiological pH, to 0.81 A resolution. Comparisons of the catalytic triad confirm the conserved position of the catalytic residues in an unoccupied active site, and demonstrate great mobility of the catalytic serine. The two conformations of the catalytic serine show some conformational fluidity in the active site of unliganded trypsin. The hydrogen-bonding network between the residues of the catalytic triad and neighbouring bonding partners is seen in the majority of serine protease structures determined to date, implying that much of this network is maintained in the unliganded state

Saccharopolyspora erythraea

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	P24664	-	-

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Release 2023.1 (January 2023)