PDBe 5hih

X-ray diffraction
1.66Å resolution

Crystal structure of the macro domain in Middle-East Respiratory Syndrome Coronavirus

Released:

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Papain-like proteinase Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 18.1 KDa
Source organism: Middle East respiratory syndrome-related coronavirus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: K9N638 (Residues: 1109-1275; Coverage: 4%)
Gene name: 1a
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Unit cell:
a: 31.58Å b: 65.17Å c: 90.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 0.141 0.177
Expression system: Escherichia coli BL21(DE3)