1uw7

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
ATP + H(2)O = ADP + phosphate
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).
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-structural protein 9 Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16 KDa
Source organism: SARS coronavirus HKU-39849
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6X7 (Residues: 4118-4230; Coverage: 2%)
Gene names: 1a-1b, rep
Sequence domains: Coronavirus replicase NSP9
Structure domains: Replicase NSP9

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P4322
Unit cell:
a: 58Å b: 58Å c: 85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.314
Expression system: Escherichia coli