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Structure of Papain


A three-dimensional X-ray study at a resolution of 2.8 Å has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft. The active site, consisting of a cysteine and a histidine, lies at the surface of the cleft. Apart from four short α-helical segments and one short segment of β-structure, the conformation of the chain is irregular.

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DRENTH, J., JANSONIUS, J., KOEKOEK, R. et al. Structure of Papain. Nature 218, 929–932 (1968).

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