1DBI
CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE
Summary for 1DBI
Entry DOI | 10.2210/pdb1dbi/pdb |
Descriptor | AK.1 SERINE PROTEASE, CALCIUM ION, SODIUM ION, ... (4 entities in total) |
Functional Keywords | hydrolase |
Biological source | Bacillus sp. AK1 |
Cellular location | Secreted: Q45670 |
Total number of polymer chains | 1 |
Total formula weight | 29932.62 |
Authors | Smith, C.A.,Toogood, H.S.,Baker, H.M.,Daniel, R.M.,Baker, E.N. (deposition date: 1999-11-02, release date: 1999-11-18, Last modification date: 2017-10-04) |
Primary citation | Smith, C.A.,Toogood, H.S.,Baker, H.M.,Daniel, R.M.,Baker, E.N. Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution. J.Mol.Biol., 294:1027-1040, 1999 Cited by PubMed: 10588904DOI: 10.1006/jmbi.1999.3291 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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