1p9s

X-ray diffraction
2.54Å resolution

Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of anti-SARS Drugs

Released:

Function and Biology Details

Reaction catalysed:
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).
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like proteinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 300 amino acids
Theoretical weight: 33.31 KDa
Source organism: Human coronavirus 229E
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6U2 (Residues: 2966-3265; Coverage: 7%)
Gene name: 1a
Sequence domains: Coronavirus endopeptidase C30
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 53.356Å b: 76.24Å c: 73.477Å
α: 90° β: 103.7° γ: 90°
R-values:
R R work R free
0.201 0.196 0.279
Expression system: Escherichia coli