4rs4

X-ray diffraction
2.96Å resolution

Crystal structure and mutational analysis of the endoribonuclease from human coronavirus 229E

Released:
Source organism: Human coronavirus 229E
Entry authors: Huo T, Liu X, Yang C, Rao Z

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
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 hexamer (preferred)
PDBe Complex ID:
PDB-CPX-143097 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridylate-specific endoribonuclease Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 349 amino acids
Theoretical weight: 38.9 KDa
Source organism: Human coronavirus 229E
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6X1 (Residues: 6111-6458; Coverage: 5%)
Gene names: 1a-1b, rep
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 127.931Å b: 143.168Å c: 174.662Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.255
Expression system: Escherichia coli