PDBe 3phw

X-ray diffraction
2Å resolution

OTU Domain of Crimean Congo Hemorrhagic Fever Virus in complex with Ubiquitin

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-directed RNA polymerase L Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 185 amino acids
Theoretical weight: 21.01 KDa
Source organism: Crimean-Congo hemorrhagic fever virus strain IbAr10200
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6TQR6 (Residues: 1-183; Coverage: 5%)
Gene name: L
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62979 (Residues: 1-75; Coverage: 48%)
Gene names: RPS27A, UBA80, UBCEP1
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 79.44Å b: 106.17Å c: 111.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.213 0.278
Expression system: Escherichia coli