X-ray diffraction
3.2Å resolution

Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
3C proteinase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 209 amino acids
Theoretical weight: 22.41 KDa
Source organism: Foot-and-mouth disease virus - type SAT 2
Expression system: Escherichia coli BL21(DE3)
  • Canonical: X5CZS0 (Residues: 714-921; Coverage: 15%)
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: ESRF BEAMLINE ID23-2
Spacegroup: P32
Unit cell:
a: 53.98Å b: 53.98Å c: 318.531Å
α: 90° β: 90° γ: 120°
R R work R free
0.225 0.222 0.272
Expression system: Escherichia coli BL21(DE3)