PDBe 4wur

X-ray diffraction
3.16Å resolution

The crystal structure of the MERS-CoV papain-like protease (C111S) with human ubiquitin

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Papain-like proteinase Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 36.16 KDa
Source organism: Betacoronavirus England 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: K9N7C7 (Residues: 1482-1801; Coverage: 5%)
Gene names: 1a-1b, rep
Structure domains:
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P63
Unit cell:
a: 138.144Å b: 138.144Å c: 57.591Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.208 0.252
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli