Function and Biology Details
Reaction catalysed:
Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero 360-mer (preferred)
Assembly name:
Membrane-lytic peptide gamma (preferred)
PDBe Complex ID:
PDB-CPX-146356 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Capsid protein beta
Molecule details ›
Chains: A, B, C
Length: 355 amino acids
Theoretical weight: 38.51 KDa
Source organism: Nodamura virus
Expression system: Galleria mellonella
UniProt:
Sequence domains: Peptidase A6 family
Structure domains: Jelly Rolls
Length: 355 amino acids
Theoretical weight: 38.51 KDa
Source organism: Nodamura virus
Expression system: Galleria mellonella
UniProt:
- Canonical:
P12871 (Residues: 1-355; Coverage: 89%)
Sequence domains: Peptidase A6 family
Structure domains: Jelly Rolls
Membrane-lytic peptide gamma
Molecule details ›
Chains: D, E, F
Length: 44 amino acids
Theoretical weight: 4.62 KDa
Source organism: Nodamura virus
UniProt:
Length: 44 amino acids
Theoretical weight: 4.62 KDa
Source organism: Nodamura virus
UniProt:
- Canonical: P12871 (Residues: 356-399; Coverage: 11%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
CHESS BEAMLINE F1
Spacegroup:
P21
Expression system: Galleria mellonella
