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]
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:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PEDV main protease (preferred)
PDBe Complex ID:
PDB-CPX-125538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PEDV main protease
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 33.3 KDa
Source organism: Porcine epidemic diarrhea virus
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Length: 305 amino acids
Theoretical weight: 33.3 KDa
Source organism: Porcine epidemic diarrhea virus
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
K4L9I6 (Residues: 2998-3295; Coverage: 4%)
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRF BEAMLINE BL17U
Spacegroup:
P21
Expression system: Escherichia coli BL21
