1uch
From Proteopedia
|
DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION
Overview
Ubiquitin C-terminal hydrolases catalyze the removal of adducts from the, C-terminus of ubiquitin. We have determined the crystal structure of the, recombinant human Ubiquitin C-terminal Hydrolase (UCH-L3) by X-ray, crystallography at 1.8 A resolution. The structure is comprised of a, central antiparallel beta-sheet flanked on both sides by alpha-helices., The beta-sheet and one of the helices resemble the well-known papain-like, cysteine proteases, with the greatest similarity to cathepsin B. This, similarity includes the UCH-L3 active site catalytic triad of Cys95, His169 and Asp184, and the oxyanion hole residue Gln89. Papain and UCH-L3, differ, however, in strand and helix connectivity, which in the UCH-L3, structure includes a disordered 20 residue loop (residues 147-166) that is, ... [(full description)]
About this Structure
1UCH is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Ubiquitin thiolesterase], with EC number [3.1.2.15]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution., Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP, EMBO J. 1997 Jul 1;16(13):3787-96. PMID:9233788
Page seeded by OCA on Tue Oct 30 13:39:37 2007
