5eyi

X-ray diffraction
2.16Å resolution

Structure of PRRSV apo-NSP11 at 2.16A

Released:
Source organism: PRRSV 16244B

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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).
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-195516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridylate-specific endoribonuclease nsp11 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 24.96 KDa
Source organism: PRRSV 16244B
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YN02 (Residues: 3586-3808; Coverage: 6%)
Gene names: 1a-1b, rep
Sequence domains: Coronavirus replicase NSP15, uridylate-specific endoribonuclease

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P41212
Unit cell:
a: 75.299Å b: 75.299Å c: 199.489Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.21
Expression system: Escherichia coli