X-ray diffraction
2.85Å resolution

Diversity of ubiquitin and ISG15 specificity amongst nairoviruses viral ovarian tumor domain proteases


Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: A, C
Molecule details ›
Chains: A, C
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P0CG48 (Residues: 609-683; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
RNA-directed RNA polymerase L Chains: B, D
Molecule details ›
Chains: B, D
Length: 174 amino acids
Theoretical weight: 20.01 KDa
Source organism: Dugbe virus (isolate ArD44313)
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q66431 (Residues: 2-169; Coverage: 4%)
Gene name: L
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 113.508Å b: 39.991Å c: 114.189Å
α: 90° β: 97.33° γ: 90°
R R work R free
0.214 0.21 0.278
Expression system: Escherichia coli BL21(DE3)