1wno

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spinqualitylabelsall models 1wno, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407

Overview

Chitinase hydrolyzes chitin, a linear polymer of beta-1,4-linked, N-acetylglucosamine (NAG), and plays a variety of roles in the biological, world. In addition to endo- and exo-hydrolytic activities, transglycosyl, activity has also been observed in the extracellular chitinase (afCHI), from the airborne saprophytic fungi Aspergillus fumigatus YJ-407. Crystals, of this native chitinase have been grown at 291 K using PEG 3350 as a, precipitant. The diffraction data from the crystal extend to 1.7 A, resolution at BSRF, China. The crystal belongs to space group, P2(1)2(1)2(1), with unit-cell parameters a = 95.7, b = 100.5, c = 134.3 A., The presence of two molecules per asymmetric unit gives a crystal volume, per protein mass (V(M)) of 3.6 A(3) Da(-1) and a solvent content of 65% by, volume. A full set of X-ray diffraction data was collected to 2.1 A, resolution.

About this Structure

1WNO is a Single protein structure of sequence from Aspergillus fumigatus with NDG, NAG, SO4 and MG as ligands. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.

Reference

Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407., Hu H, Wang G, Yang H, Zhou J, Mo L, Yang K, Jin C, Jin C, Rao Z, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):939-40. Epub 2004, Apr 21. PMID:15103145

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