PDBe 2bx4

X-ray diffraction
2.79Å resolution

Crystal Structure of SARS Coronavirus Main Proteinase (P21212)

Released:

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate. 
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). 
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position. 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like proteinase Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 33.88 KDa
Source organism: SARS coronavirus Sin2774
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6X7 (Residues: 3241-3546; Coverage: 4%)
Gene names: 1a-1b, rep
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 108.23Å b: 44.557Å c: 54.198Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.208 0.302
Expression system: Escherichia coli