1l1n

X-ray diffraction
2.1Å resolution

POLIOVIRUS 3C PROTEINASE

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease 3C Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 19.65 KDa
Source organism: Human poliovirus 1 Mahoney
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P03300 (Residues: 1566-1748; 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 RU200
Spacegroup: P212121
Unit cell:
a: 79.26Å b: 116.31Å c: 47.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.259
Expression system: Escherichia coli BL21