1lvo

X-ray diffraction
1.96Å resolution

Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain

Released:

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
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).
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-143140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like proteinase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 302 amino acids
Theoretical weight: 33.12 KDa
Source organism: Transmissible gastroenteritis virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6Y5 (Residues: 2879-3180; Coverage: 5%)
Gene names: 1a-1b, rep
Sequence domains: Coronavirus endopeptidase C30
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A, ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 72.82Å b: 160.13Å c: 88.96Å
α: 90° β: 94.3° γ: 90°
R-values:
R R work R free
0.21 0.21 0.256
Expression system: Escherichia coli