CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.390 | Collagenase (Catalytic Domain) |
|
3.40.390.10 | Collagenase (Catalytic Domain) |
Domain Context
CATH Clusters
| Superfamily | Collagenase (Catalytic Domain) |
| Functional Family | Neutral protease 2 |
Enzyme Information
| 3.4.24.39 |
Deuterolysin.
based on mapping to UniProt P46076
Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.
-!- Proteolytic activity found in Penicillium roqueforti, P.caseicolum, Aspergillus sojae and A.oryzae. -!- Optimum pH of 5 for digesting various proteins. -!- Strong action on protamine and histones. -!- Insensitive to phosphoramidon. -!- A distinct A.sojae endopeptidase is larger and has neutral pH optimum. -!- Belongs to peptidase family M35. -!- Formerly EC 3.4.24.4.
|
UniProtKB Entries (1)
| P46076 |
NPII_ASPOR
Aspergillus oryzae RIB40
Neutral protease 2
|
PDB Structure
| PDB | 1EB6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A Quick Solution: Ab Initio Structure Determination of a 19 kDa Metalloproteinase Using Acorn
Acta Crystallogr.,Sect.D
|