› 3zvg

X-ray diffraction
2.1Å resolution

3C protease of Enterovirus 68 complexed with Michael receptor inhibitor 98

Released:
DOI: 10.2210/pdb3zvg/pdb
PDB entry 3zvg coloured by chain, front view.
PDB entry 3zvg coloured by chain, side view.
PDB entry 3zvg coloured by chain, top view.
Source organism: enterovirus D68
Primary publication:
3C protease of enterovirus 68: structure-based design of Michael acceptor inhibitors and their broad-spectrum antiviral effects against picornaviruses.
Tan J, George S, Kusov Y, Perbandt M, Anemüller S, Mesters JR, Norder H, Coutard B, Lacroix C, Leyssen P, Neyts J, Hilgenfeld R
J Virol 87 4339-51 (2013)
PMID: 23388726

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
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C PROTEASE Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.16 KDa
Source organism: enterovirus D68
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A1E4A3 (Residues: 1549-1731; Coverage: 8%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand G86 1 x G86
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3121
Unit cell:
a: 56.2Å b: 56.2Å c: 170.231Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.198 0.237
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design.
Hilgenfeld R. (2014)
15 more

2 mentions without citation

3C protease of enterovirus 68: structure-based design of Michael acceptor inhibitors and their broad-spectrum antiviral effects against picornaviruses.
Tan et al. (2013)
1 more