6vgy

X-ray diffraction
2.05Å resolution

2.05 A resolution structure of MERS 3CL protease in complex with inhibitor 6b

Released:

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
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:
ORF1ab Chains: A, B
Molecule details ›
Chains: A, B
Length: 313 amino acids
Theoretical weight: 34.31 KDa
Source organism: Middle East respiratory syndrome-related coronavirus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: T2B9U0 (Residues: 3248-3553; Coverage: 4%)
Sequence domains: Coronavirus endopeptidase C30

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 76.139Å b: 91.669Å c: 100.703Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.239
Expression system: Escherichia coli BL21