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Summary
| Description |
An early (1984) X-ray crystallography structure of papain, a cysteine protease enzyme found in papaya. The primarily alpha-helical L-domain is shown at left, while the beta-sheet-rich R-domain is shown at right. The catalytic residues are highlighted; cysteine (oxidized in this structure) in green and histidine in blue. A conserved disulfide bond is shown in cyan. Rendered using PyMol from PDB: 9PAP. Structure of papain refined at 1.65 A resolution Kamphuis, I.G., Kalk, K.H., Swarte, M.B., Drenth, J. (1984) J Mol Biol 179: 233-256 PubMed: 6502713 DOI: 10.1016/0022-2836(84)90467-4 |
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| Source | Own work |
| Author | Opabinia regalis |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 06:05, 28 December 2021 | | 800 × 600 (266 KB) | Opabinia regalis | {{Information |Description=An early (1984) X-ray crystallography structure of papain, a cysteine protease enzyme found in papaya. The primarily alpha-helical L-domain is shown at left, while the beta-sheet-rich R-domain is shown at right. The catalytic residues are highlighted; cysteine (oxidized in this structure) in green and histidine in blue. A conserved disulfide bond is shown in cyan. Rendered using PyMol from {{PDB|9PAP}}. Structure of papain refined at 1.65 A resolution Kamphuis, I.G... |
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