Function and Biology Details
Reaction catalysed:
Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Neutral protease 2 (preferred)
PDBe Complex ID:
PDB-CPX-155422 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutral protease 2
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 19.03 KDa
Source organism: Aspergillus oryzae
UniProt:
Sequence domains: Deuterolysin metalloprotease (M35) family
Structure domains: Collagenase (Catalytic Domain)
Length: 177 amino acids
Theoretical weight: 19.03 KDa
Source organism: Aspergillus oryzae
UniProt:
- Canonical:
P46076 (Residues: 176-352; Coverage: 53%)
Sequence domains: Deuterolysin metalloprotease (M35) family
Structure domains: Collagenase (Catalytic Domain)
