Function and Biology Details
Reaction catalysed:
Autocatalytic release of the core protein from the N-terminus of thetogavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Capsid protein (preferred)
PDBe Complex ID:
PDB-CPX-183110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.01 KDa
Source organism: Aura virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 158 amino acids
Theoretical weight: 17.01 KDa
Source organism: Aura virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q86925 (Residues: 110-267; Coverage: 13%)
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
BRUKER AXS MICROSTAR-H
Spacegroup:
C2
Expression system: Escherichia coli BL21(DE3)
