1bpl
From Proteopedia
|
GLYCOSYLTRANSFERASE
Overview
The three-dimensional structure of the calcium-free form of Bacillus, licheniformis alpha-amylase (BLA) has been determined by multiple, isomorphous replacement in a crystal of space group P4(3)2(1)2 (a = b =, 119.6 A, c = 85.4 A). The structure was refined using restrained, crystallographic refinement to an R-factor of 0.177 for 28,147 independent, reflections with intensities FObs > 0 at 2.2 A resolution, with root mean, square deviations of 0.008 A and 1.4 degrees from ideal bond lengths and, bond angles, respectively. The final model contains 469 residue, 237 water, molecules, and one chloride ion. The segment between Trp182 and Asn192, could not be located in the electron density, nor could the N and C, termini. Cleavage of the calcium-free form of BLA was observed after, Glu189, ... [(full description)]
About this Structure
1BPL is a [Protein complex] structure of sequences from [Bacillus licheniformis]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution., Machius M, Wiegand G, Huber R, J Mol Biol. 1995 Mar 3;246(4):545-59. PMID:7877175
Page seeded by OCA on Tue Oct 30 14:56:32 2007
