1SCD

X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE

Summary for 1SCD

Entry DOI	10.2210/pdb1scd/pdb
Descriptor	SUBTILISIN CARLSBERG, CALCIUM ION (3 entities in total)
Functional Keywords	serine protease
Biological source	Bacillus licheniformis
Cellular location	Secreted: P00780
Total number of polymer chains	1
Total formula weight	27386.35
Authors	Fitzpatrick, P.A.,Ringe, D.,Klibanov, A.M. (deposition date: 1993-08-23, release date: 1994-01-31, Last modification date: 2024-02-14)
Primary citation	Fitzpatrick, P.A.,Ringe, D.,Klibanov, A.M. X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile. Biochem.Biophys.Res.Commun., 198:675-681, 1994 Cited by PubMed Abstract: The crystal structure of subtilisin Carlsberg lightly cross-linked with glutaraldehyde was solved in aqueous solution by X-ray crystallography at 2.3 A resolution. It was found to be virtually identical to the recently determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the cross-linked enzyme in anhydrous acetonitrile. The latter structure was found to be significantly more rigid than in water, as reflected by their average B factors. The numbers of subtilisin-bound water molecules in the two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are distinct. PubMed: 8297378 DOI: 10.1006/bbrc.1994.1098 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation