Structure of Papain

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 1968 English Publisher:Springer Science and Business Media LLCJournal:Nature, volume 218, pages 929-932 (issn: 0028-0836, eissn: 1476-4687,

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Authors: J, Drenth; J N, Jansonius; R, Koekoek; H M, Swen; B G, Wolthers;

doi: 10.1038/218929a0

pmid: 5681232

Structure of Papain

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Abstract

A three-dimensional X-ray study at a resolution of 2.8 A 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.

Related Organizations

University of Groningen
Netherlands

Keywords

Absorptiometry, Photon, Binding Sites, Lysine, Papain, Tyrosine, Amino Acid Sequence, Peptides, Thiocyanates

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