1uk3

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spinqualitylabelsall models PDB ID 1uk3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.4Å
Related:	1UK2, 1UK4
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Crystal structure of SARS Coronavirus Main Proteinase (3CLpro) At pH7.6

Overview

A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.

About this Structure

1UK3 is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

Reference

The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor., Yang H, Yang M, Ding Y, Liu Y, Lou Z, Zhou Z, Sun L, Mo L, Ye S, Pang H, Gao GF, Anand K, Bartlam M, Hilgenfeld R, Rao Z, Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13190-5. Epub 2003 Oct 29. PMID:14585926

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