1sup
From Proteopedia
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SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS
Overview
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.
About this Structure
1SUP is a Single protein structure of sequence from Bacillus amyloliquefaciens with CA, NA and PMS as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
Subtilisin BPN' at 1.6 A resolution: analysis for discrete disorder and comparison of crystal forms., Gallagher T, Oliver J, Bott R, Betzel C, Gilliland GL, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1125-35. PMID:15299573
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