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; PubMed: 2684274; DOI: 10.1021/bi00444a012

Experimental method

X-RAY DIFFRACTION (1.7 Å)