CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.128 | Lipocalin |
|
2.40.128.80 | Cathepsin C, exclusion domain |
Domain Context
CATH Clusters
| Superfamily | Cathepsin C, exclusion domain |
| Functional Family | Dipeptidyl peptidase 1 |
Enzyme Information
| 3.4.14.1 |
Dipeptidyl-peptidase I.
based on mapping to UniProt P53634
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
-!- Also polymerizes dipeptide amides, arylamides and esters at neutral pH. -!- Cl(-)-dependent lysosomal cysteine-type peptidase. -!- Belongs to peptidase family C1. -!- Formerly EC 3.4.4.9.
|
UniProtKB Entries (1)
| P53634 |
CATC_HUMAN
Homo sapiens
Dipeptidyl peptidase 1
|
PDB Structure
| PDB | 4OEL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The amino-acid substituents of dipeptide substrates of cathepsin C can determine the rate-limiting steps of catalysis.
Biochemistry
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