1bh6
From Proteopedia
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| - | [[Image:1bh6.gif|left|200px]]<br /> | + | [[Image:1bh6.gif|left|200px]]<br /><applet load="1bh6" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bh6" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1bh6, resolution 1.75Å" /> | caption="1bh6, resolution 1.75Å" /> | ||
'''SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE'''<br /> | '''SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BH6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with CA, NA and 1BH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] | + | 1BH6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with CA, NA and 1BH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Known structural/functional Site: <scene name='pdbsite=ACT:Active Site'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BH6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:26:49 2007'' |
Revision as of 12:17, 18 December 2007
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SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE
Overview
The crystal structure of subtilisin DY inhibited by, N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by, molecular replacement with subtilisin Carlsberg as the starting model. The, model has been refined to a crystallographic R factor (= sigma absolute, value [(absolute value Fo) - (absolute value Fc)] / sigma (absolute value, of Fo) of 15.1% using X-ray diffraction data to 0.175 nm resolution., Subtilisin DY is an alkaline proteinase from the X-irradiated Japanese, strain DY of Bacillus licheniformis, which normally produces subtilisin, Carlsberg. It has very similar properties to subtilisin Carlsberg, with a, slightly enhanced resistance to heat and guanidine hydrochloride-induced, denaturation, in spite of the fact that the sequences of the two enzymes, differ in 31 positions out of 274 residues. The close similarity in, overall three-dimensional structure of subtilisins DY and Carlsberg and, also their physicochemical properties, such as activity and stability, shows that nature aided by X-irradiation for rapid 'evolution' is able to, accommodate considerable changes in sequence without substantial changes, in property.
About this Structure
1BH6 is a Single protein structure of sequence from Bacillus licheniformis with CA, NA and 1BH as ligands. Active as Subtilisin, with EC number 3.4.21.62 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg., Eschenburg S, Genov N, Peters K, Fittkau S, Stoeva S, Wilson KS, Betzel C, Eur J Biochem. 1998 Oct 15;257(2):309-18. PMID:9826175
Page seeded by OCA on Tue Dec 18 14:26:49 2007
Categories: Bacillus licheniformis | Single protein | Subtilisin | Betzel, C. | Eschenburg, S. | Genov, N. | Wilson, K.S. | 1BH | CA | NA | Hydrolase | Protein degradation
