3tlo

X-ray diffraction
1.6Å resolution

Crystal structure of HCoV-NL63 3C-like protease

Released:
Source organism: Human coronavirus NL63
Entry authors: Chuck CP, Wong KB

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like proteinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 32.76 KDa
Source organism: Human coronavirus NL63
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6U6 (Residues: 2940-3242; Coverage: 8%)
Gene name: 1a
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 63.144Å b: 83.497Å c: 64.852Å
α: 90° β: 109.2° γ: 90°
R-values:
R R work R free
0.176 0.175 0.202
Expression system: Escherichia coli