1S01
LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING
Summary for 1S01
Entry DOI | 10.2210/pdb1s01/pdb |
Descriptor | Subtilisin BPN', CALCIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total) |
Functional Keywords | hydrolase (serine proteinase), hydrolase |
Biological source | Bacillus amyloliquefaciens (Bacillus velezensis) |
Cellular location | Secreted: P00782 |
Total number of polymer chains | 1 |
Total formula weight | 27703.87 |
Authors | Whitlow, M.,Howard, A.J.,Wood, J.F. (deposition date: 1989-08-21, release date: 1990-10-15, Last modification date: 2018-02-14) |
Primary citation | Pantoliano, M.W.,Whitlow, M.,Wood, J.F.,Dodd, S.W.,Hardman, K.D.,Rollence, M.L.,Bryan, P.N. Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Biochemistry, 28:7205-7213, 1989 Cited by PubMed: 2684274DOI: 10.1021/bi00444a012 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report