2PNS
1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C refinement with cDNA derived amino acid sequence
Summary for 2PNS
Entry DOI | 10.2210/pdb2pns/pdb |
Related | 1O0E |
Descriptor | Ervatamin-C, a papain-like plant cysteine protease, PHOSPHATE ION, THIOSULFATE, ... (4 entities in total) |
Functional Keywords | papain-like fold, thermostable, plant cysteine protease, ervatamin, hydrolase |
Biological source | Tabernaemontana divaricata |
Cellular location | Secreted: P83654 |
Total number of polymer chains | 2 |
Total formula weight | 46307.89 |
Authors | Ghosh, R.,Guha Thakurta, P.,Biswas, S.,Chakrabarti, C.,Dattagupta, J.K. (deposition date: 2007-04-25, release date: 2007-06-19, Last modification date: 2023-08-30) |
Primary citation | Ghosh, R.,Dattagupta, J.K.,Biswas, S. A thermostable cysteine protease precursor from a tropical plant contains an unusual C-terminal propeptide: cDNA cloning, sequence comparison and molecular modeling studies. Biochem.Biophys.Res.Commun., 362:965-970, 2007 Cited by PubMed: 17767923DOI: 10.1016/j.bbrc.2007.08.098 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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