5v5g

X-ray diffraction
2.1Å resolution

OTU protease of Crimean Congo Hemorrhagic Fever Virus bound to ubiquitin variant CC.4

Released:

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)
PDBe Complex ID:
PDB-CPX-166193 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-directed RNA polymerase L Chains: A, C
Molecule details ›
Chains: A, C
Length: 186 amino acids
Theoretical weight: 21.08 KDa
Source organism: Crimean-Congo hemorrhagic fever virus strain IbAr10200
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6TQR6 (Residues: 1-183; Coverage: 5%)
Gene name: L
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin variant CC.4 Chains: B, D
Molecule details ›
Chains: B, D
Length: 105 amino acids
Theoretical weight: 12.1 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P43212
Unit cell:
a: 64.312Å b: 64.312Å c: 277.578Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.174 0.229
Expression system: Escherichia coli BL21(DE3)