3ewp

X-ray diffraction
2Å resolution

complex of substrate ADP-ribose with IBV Nsp3 ADRP domain

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

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Papain-like protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 177 amino acids
Theoretical weight: 19.2 KDa
Source organism: Infectious bronchitis virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6V5 (Residues: 1005-1178; Coverage: 4%)
Gene name: 1a
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P1
Unit cell:
a: 41.364Å b: 43.985Å c: 49.266Å
α: 78.25° β: 79.45° γ: 73.39°
R-values:
R R work R free
0.178 0.176 0.23
Expression system: Escherichia coli