Title : Three-dimensional structure of proteinase K at 0.15-nm resolution.

Pub. Date : 1988 Dec 1

PMID : 3203685






1 Functional Relationships(s)
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Protein Name
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1 Based on these experiments, a reaction mechanism is proposed where the peptide substrate forms a three-stranded antiparallel pleated sheet with the recognition site of proteinase K consisting of Ser132--Leu133--Gly134 on one side and Gly100--Ser101 on the other, followed by expulsion of the oxyanion hole water W335 and hydrolytic cleavage by the Asp39--His69--Serr224 triad. serr224 endogenous retrovirus group K member 7 Homo sapiens