5hbz

X-ray diffraction
3.1Å resolution

Structure of EAV NSP11 K170A mutant at 3.10A

Released:

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-148744 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridylate-specific endoribonuclease nsp11 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 221 amino acids
Theoretical weight: 24.36 KDa
Source organism: Equine arteritis virus Bucyrus
Expression system: Escherichia coli
UniProt:
  • Canonical: P19811 (Residues: 2838-3056; Coverage: 7%)
Gene names: 1a-1b, rep
Sequence domains: Coronavirus replicase NSP15, uridylate-specific endoribonuclease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: R32
Unit cell:
a: 248.268Å b: 248.268Å c: 226.298Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.199
Expression system: Escherichia coli