1bh6
From Proteopedia
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|PDB= 1bh6 |SIZE=350|CAPTION= <scene name='initialview01'>1bh6</scene>, resolution 1.75Å | |PDB= 1bh6 |SIZE=350|CAPTION= <scene name='initialview01'>1bh6</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=1BH:N-BENZYLOXYCARBONYL-ALA-PRO-3-AMINO-4-PHENYL-BUTAN-2-OL'>1BH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh6 OCA], [http://www.ebi.ac.uk/pdbsum/1bh6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bh6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Genov, N.]] | [[Category: Genov, N.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
| - | [[Category: 1BH]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NA]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: protein degradation]] | [[Category: protein degradation]] | ||
[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:53 2008'' |
Revision as of 16:00, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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