CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.10 | Thrombin, subunit H |
|
2.40.10.10 | Trypsin-like serine proteases |
Domain Context
CATH Clusters
| Superfamily | Trypsin-like serine proteases |
| Functional Family | Complement C1r subcomponent |
Enzyme Information
| 3.4.21.41 |
Complement subcomponent C1r.
based on mapping to UniProt P00736
Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).
-!- Activates C1s by proteolytic cleavage so that it can, in turn, activate C2 and C4. -!- Activated from proenzyme C1r in plasma by autocatalytic mechanism during activation of the complement system by the 'classical' route. -!- Belongs to peptidase family S1.
|
UniProtKB Entries (1)
| P00736 |
C1R_HUMAN
Homo sapiens
Complement C1r subcomponent
|
PDB Structure
| PDB | 1GPZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Crystal Structure of the Zymogen Catalytic Domain of Complement Protease C1R Reveals that a Disruptive Mechanical Stress is Required to Trigger Activation of the C1 Complex.
Embo J.
|
