PDBe 3prm

X-ray diffraction
2.3Å resolution

Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin

Released:

Function and Biology Details

Reaction 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).
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):
L protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 178 amino acids
Theoretical weight: 20.57 KDa
Source organism: Crimean-Congo hemorrhagic fever orthonairovirus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6TFZ7 (Residues: 1-170; Coverage: 4%)
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • 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

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 60.462Å b: 65.651Å c: 133.133Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.204 0.267
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli BL21