PDBe 2b0f

Solution NMR

NMR Structure of the Human Rhinovirus 3C Protease (serotype 14) with covalently bound Ace-LEALFQ-ethylpropionate inhibitor

Released:

Function and Biology Details

Reactions catalysed:
NTP + H(2)O = NDP + phosphate. 
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly. 
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ace-LEALFQ-ethylpropionate Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 830 Da
Source organism: Synthetic construct
Expression system: Not provided
Protease 3C Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 20.02 KDa
Source organism: Rhinovirus B14
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03303 (Residues: 1538-1719; Coverage: 8%)
Sequence domains: 3C cysteine protease (picornain 3C)
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing molecular dynamics torsion angle dynamics RECOORD water refinement
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)