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Structure paper

TitleLarge increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.
Journal, issue, pagesBiochemistry, Vol. 28, Page 7205-7213, Year 1989
Publish dateJan 8, 1998 (structure data deposition date)
AuthorsPantoliano, M.W. / Whitlow, M. / Wood, J.F. / Dodd, S.W. / Hardman, K.D. / Rollence, M.L. / Bryan, P.N.
External linksBiochemistry / PubMed:2684274
MethodsX-ray diffraction
Resolution1.7 - 1.8 Å
Structure data

PDB-1a2q:
SUBTILISIN BPN' MUTANT 7186
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1ak9:
SUBTILISIN MUTANT 8321
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1au9:
SUBTILISIN BPN' MUTANT 8324 IN CITRATE
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1s01:
LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ACN:
ACETONE

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-IPA:
ISOPROPYL ALCOHOL

ChemComp-UNX:
Unknown entry

Source
  • bacillus amyloliquefaciens (bacteria)
KeywordsHYDROLASE / SERINE PROTEASE / SPORULATION / HYDROLASE (SERINE PROTEINASE)

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