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1uch
From Proteopedia
(New page: 200px<br /> <applet load="1uch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uch, resolution 1.80Å" /> '''DEUBIQUITINATING EN...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1UCH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UCH OCA]]. | + | 1UCH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UCH OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Ubiquitin thiolesterase]] | ||
[[Category: Cook, W.J.]] | [[Category: Cook, W.J.]] | ||
[[Category: Hill, C.P.]] | [[Category: Hill, C.P.]] | ||
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[[Category: ubiquitin conjugation]] | [[Category: ubiquitin conjugation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:39:37 2007'' |
Revision as of 11:34, 30 October 2007
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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
