› 2ztz

X-ray diffraction
2Å resolution

crystal structure of 3C protease from CVB3 in space group P21

Released:
DOI: 10.2210/pdb2ztz/pdb
PDB entry 2ztz coloured by chain, front view.
PDB entry 2ztz coloured by chain, side view.
PDB entry 2ztz coloured by chain, top view.
Source organism: Coxsackievirus B3
Primary publication:
Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.
Lee CC, Kuo CJ, Ko TP, Hsu MF, Tsui YC, Chang SC, Yang S, Chen SJ, Chen HC, Hsu MC, Shih SR, Liang PH, Wang AH
OpenAccess logo J Biol Chem 284 7646-55 (2009)
PMID: 19144641

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-136767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.3 KDa
Source organism: Coxsackievirus B3
Expression system: Escherichia coli
UniProt:
  • Canonical: P03313 (Residues: 1541-1723; Coverage: 8%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002
Spacegroup: P21
Unit cell:
a: 38.88Å b: 64.52Å c: 68.28Å
α: 90° β: 90.58° γ: 90°
R-values:
R R work R free
0.169 0.166 0.237
Expression system: Escherichia coli

Quick links

Citations

20 review citations

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

2 mentions without citation

Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.
Lee et al. (2009)
1 more