X-ray diffraction
2.59Å resolution

Crystal structure of PLpro from Middle East Respiratory Syndrome (MERS) coronavirus

Entry authors: Lei H, Santarsiero BD, Lee H, Johnson ME

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:
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: 324 amino acids
Theoretical weight: 36.04 KDa
Source organism: Human betacoronavirus 2c EMC/2012
Expression system: Escherichia coli BL21
  • Canonical: K4LC41 (Residues: 1482-1803; Coverage: 7%)
Gene name: orf1ab
Structure domains:

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 100.82Å b: 47.26Å c: 88.77Å
α: 90° β: 121.6° γ: 90°
R R work R free
0.232 0.229 0.299
Expression system: Escherichia coli BL21