PDBe 5wkl

X-ray diffraction
1.85Å resolution

1.85 A resolution structure of MERS 3CL protease in complex with piperidine-based peptidomimetic inhibitor 17


Function and Biology Details

Reactions 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).
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.
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
3C-like proteinase Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 34.31 KDa
Source organism: Middle East respiratory syndrome-related coronavirus
Expression system: Escherichia coli BL21
  • Canonical: K9N638 (Residues: 3248-3553; Coverage: 7%)
Gene name: 1a

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 101.253Å b: 58.099Å c: 49.734Å
α: 90° β: 112° γ: 90°
R R work R free
0.166 0.163 0.212
Expression system: Escherichia coli BL21