Structure of a proteolytically resistant analogue of (NLys)5SFTI-1 in complex with trypsin: evidence for the direct participation of the Ser214 carbonyl group in serine protease-mediated proteolysis

Krzywda, S.; Jaskolski, M.; Rolka, K.; Stawikowski, M.J.

doi:10.1107/S1399004713032252

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 4
Comparison of the side chains of the NLys5 residue (thick, magenta; this work) and the Lys5 residue of the native inhibitor (thick, cyan; PDB entry 1sfi ) after C^α superposition of their trypsin complexes. The terminal ∊-NH₃⁺ group of NLys5 makes the same contacts (dashed lines) with the bottom of the catalytic pocket of the enzyme, including hydrogen bonds to two water molecules (WAT; red balls). An analysis of the side-chain χ angles of P1 residues is presented in Supplementary Table S1.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 668-675

doi:10.1107/S1399004713032252

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