PDBe 5e6j

X-ray diffraction
2.85Å resolution

Structure of SARS PLpro bound to a Lys48-linked di-ubiquitin activity based probe

Released:

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate
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).
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Papain-like proteinase Chains: A, D
Molecule details ›
Chains: A, D
Length: 325 amino acids
Theoretical weight: 36.69 KDa
UniProt:
  • Canonical: P0C6X7 (Residues: 1541-1856; Coverage: 5%)
Gene names: 1a-1b, rep
Structure domains:
Ubiquitin Chains: B, E
Molecule details ›
Chains: B, E
Length: 76 amino acids
Theoretical weight: 8.62 KDa
Source organism: synthetic construct
Expression system: Not provided
UniProt:
  • Canonical: P0CG48 (Residues: 609-683; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Ubiquitin Chains: C, F
Molecule details ›
Chains: C, F
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: synthetic construct
Expression system: Not provided
UniProt:
  • Canonical: P0CG47 (Residues: 153-227; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 72.981Å b: 68.239Å c: 119.021Å
α: 90° β: 103.21° γ: 90°
R-values:
R R work R free
0.234 0.232 0.264
Expression system: Not provided