1SUP

SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS

Summary for 1SUP

• Entry DOI: 10.2210/pdb1sup/pdb
• Descriptor: SUBTILISIN BPN', CALCIUM ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase (serine protease)
• Biological source: Bacillus amyloliquefaciens
• Cellular location: Secreted: P00782
• Total number of polymer chains: 1
• Total formula weight: 27787.80

Authors

Gallagher, D.T.,Oliver, J.D.,Betzel, C.,Gilliland, G.L. (deposition date: 1995-08-14, release date: 1995-11-14, Last modification date: 2024-12-25)

Primary citation

Gallagher, T.,Oliver, J.,Bott, R.,Betzel, C.,Gilliland, G.L.
Subtilisin BPN' at 1.6 A resolution: analysis for discrete disorder and comparison of crystal forms.
Acta Crystallogr.,Sect.D, 52:1125-1135, 1996

PubMed Abstract: The three-dimensional structure of the serine protease subtilisin BPN' (SBT) has been refined at 1.6 A resolution in space group C2 to a final R value of 0.17. 17 regions of discrete disorder have been identified and analyzed. Two of these are dual-conformation peptide units; the remainder involve alternate rotamers of side chains either alone or in small clusters. The structure is compared with previously reported high-resolution models of SBT in two other space groups, P2(1)2(1)2(1) and P2(1). Apart from the surface, there are no significant variations in structure among the three crystal forms. Structural variations observed at the protein surface occur predominantly in regions of protein-protein contact. The crystal packing arrangements in the three space groups are compared.

PubMed: 15299573
DOI: 10.1107/S0907444996007500

Experimental method

X-RAY DIFFRACTION (1.6 Å)