5tl6

X-ray diffraction
2.62Å resolution

Crystal structure of SARS-CoV papain-like protease in complex with the C-terminal domain of human ISG15

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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.
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Papain-like proteinase Chains: B, D
Molecule details ›
Chains: B, D
Length: 319 amino acids
Theoretical weight: 35.81 KDa
Source organism: Severe acute respiratory syndrome-related coronavirus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0C6X7 (Residues: 1537-1537, 1541-1855; Coverage: 5%)
Gene names: 1a-1b, rep
Ubiquitin-like protein ISG15 Chains: A, C
Molecule details ›
Chains: A, C
Length: 79 amino acids
Theoretical weight: 8.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05161 (Residues: 80-157; Coverage: 47%)
Gene names: G1P2, ISG15, UCRP
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 46.881Å b: 86.988Å c: 221.532Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.25
Expression system: Escherichia coli BL21(DE3)