Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state

Blankenship, E.; Vukoti, K.; Miyagi, M.; Lodowski, D.T.

doi:10.1107/S1399004713033658

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 2
SET exhibits the prototypical trypsin fold. The structure contains two α-helices (cyan) and 14 β-sheets (magenta). 13 β-sheets are present in the high-resolution bovine trypsin structure (PDB entry 4i8h ), and an additional β-sheet (B6) was identified during structural analysis of SET. Active-site residues are depicted as blue sticks. H atoms have been removed for clarity.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 833-840

doi:10.1107/S1399004713033658

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