PDBe 3phu

X-ray diffraction
2.2Å resolution

OTU Domain of Crimean Congo Hemorrhagic Fever Virus

Released:

Function and Biology Details

Reactions catalysed:
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).
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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
Macromolecule:
RNA-directed RNA polymerase L Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 24.76 KDa
Source organism: Crimean-Congo hemorrhagic fever virus strain IbAr10200
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6TQR6 (Residues: 1-217; Coverage: 6%)
Gene name: L
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3221
Unit cell:
a: 115.99Å b: 115.99Å c: 94.171Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.231
Expression system: Escherichia coli