4DWW
Crystal Structure of Nattokinase from Bacillus subtilis natto
Summary for 4DWW
| Entry DOI | 10.2210/pdb4dww/pdb |
| Descriptor | Subtilisin NAT, CALCIUM ION (3 entities in total) |
| Functional Keywords | fibrinolytic activity, hydrolase |
| Biological source | Bacillus subtilis subsp. natto |
| Cellular location | Secreted: P35835 |
| Total number of polymer chains | 1 |
| Total formula weight | 27978.95 |
| Authors | Chatake, T.,Yanagisawa, Y. (deposition date: 2012-02-27, release date: 2012-03-14, Last modification date: 2023-11-08) |
| Primary citation | Yanagisawa, Y.,Chatake, T.,Chiba-Kamoshida, K.,Naito, S.,Ohsugi, T.,Sumi, H.,Yasuda, I.,Morimoto, Y. Purification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto Acta Crystallogr.,Sect.F, 66:1670-1673, 2010 Cited by PubMed Abstract: Nattokinase is a single polypeptide chain composed of 275 amino acids (molecular weight 27,724) which displays strong fibrinolytic activity. Moreover, it can activate other fibrinolytic enzymes such as pro-urokinase and tissue plasminogen activator. In the present study, native nattokinase from Bacillus subtilis natto was purified using gel-filtration chromatography and crystallized to give needle-like crystals which could be used for X-ray diffraction experiments. The crystals belonged to space group C2, with unit-cell parameters a=74.3, b=49.9, c=56.3 Å, β=95.2°. Diffraction images were processed to a resolution of 1.74 Å with an Rmerge of 5.2% (15.3% in the highest resolution shell) and a completeness of 69.8% (30.0% in the highest resolution shell). This study reports the first X-ray diffraction analysis of nattokinase. PubMed: 21139221DOI: 10.1107/S1744309110043137 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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