3q3x

X-ray diffraction
1.9Å resolution

Crystal structure of the main protease (3C) from human enterovirus B EV93

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
NTP + H(2)O = NDP + phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-176978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HEVB EV93 3C protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 191 amino acids
Theoretical weight: 21.44 KDa
Source organism: Enterovirus B
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5DSM6 (Residues: 1556-1738; Coverage: 8%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 39.072Å b: 65.216Å c: 66.355Å
α: 90° β: 90.67° γ: 90°
R-values:
R R work R free
0.151 0.148 0.21
Expression system: Escherichia coli