CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.70 | Cathepsin D, subunit A; domain 1 |
|
2.40.70.10 | Acid Proteases |
Domain Context
CATH Clusters
| Superfamily | Acid Proteases |
| Functional Family |
Enzyme Information
| 3.4.23.1 |
Pepsin A.
based on mapping to UniProt P0DJD7
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
-!- The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.1.
|
UniProtKB Entries (1)
| P0DJD7 |
PEPA4_HUMAN
Homo sapiens
Pepsin A-4
|
PDB Structure
| PDB | 3UTL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.
Acta Crystallogr.,Sect.D
|
