2wbc
From Proteopedia
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REFINED CRYSTAL STRUCTURE (2.3 ANGSTROM) OF A WINGED BEAN CHYMOTRYPSIN INHIBITOR AND LOCATION OF ITS SECOND REACTIVE SITE
Overview
The crystal structure of a double-headed alpha-chymotrypsin inhibitor, WCI, from winged bean seeds has now been refined at 2.3 A resolution to an, R-factor of 18.7% for 9,897 reflections. The crystals belong to the, hexagonal space group P6(1)22 with cell parameters a = b = 61.8 A and c =, 212.8 A. The final model has a good stereochemistry and a root mean square, deviation of 0.011 A and 1.14 degrees from ideality for bond length and, bond angles, respectively. A total of 109 ordered solvent molecules were, localized in the structure. This improved structure at 2.3 A led to an, understanding of the mechanism of inhibition of the protein against, alpha-chymotrypsin. An analysis of this higher resolution structure also, helped us to predict the location of the second reactive site of the, ... [(full description)]
About this Structure
2WBC is a [Single protein] structure of sequence from [Psophocarpus tetragonolobus]. Structure known Active Sites: 1ST and 2ND. Full crystallographic information is available from [OCA].
Reference
Refined crystal structure (2.3 A) of a double-headed winged bean alpha-chymotrypsin inhibitor and location of its second reactive site., Dattagupta JK, Podder A, Chakrabarti C, Sen U, Mukhopadhyay D, Dutta SK, Singh M, Proteins. 1999 May 15;35(3):321-31. PMID:10328267
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