7vtc

X-ray diffraction
2.54Å resolution

Crystal structure of MERS main protease in complex with PF07321332

Released:
Entry authors: Lin C, Zhong FL, Zhou XL, Zhang J, Li J

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ORF1a Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 35.24 KDa
Source organism: Middle East respiratory syndrome-related coronavirus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: T2B9A8 (Residues: 3250-3548; Coverage: 7%)
Sequence domains: Coronavirus endopeptidase C30

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL02U1
Spacegroup: P212121
Unit cell:
a: 83.422Å b: 93.243Å c: 97.578Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.242
Expression system: Escherichia coli BL21