CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.10 | Ribbon |
|
2.10.70 | Complement Module; domain 1 |
|
2.10.70.10 | Complement Module, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Complement Module, domain 1 |
| Functional Family | Mannan-binding lectin serine protease 1 |
Enzyme Information
| 3.4.21.104 |
Mannan-binding lectin-associated serine protease-2.
based on mapping to UniProt O00187
Selective cleavage after Arg-223 in complement component C2 (-Ser- Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).
-!- Mannan-binding lectin (MBL) recognizes patterns of neutral carbohydrates, such as mannose and N-acetylglucosamine, on a wide range of microbial surfaces and is able to initiate activation of the lectin pathway of complement. -!- Displays C1s-like esterolytic activity (cf. EC 3.4.21.42). -!- It also cleaves C4 and C2 with efficiencies that are relatively higher than those of EC 3.4.21.42. -!- Belongs to peptidase family S1A.
|
UniProtKB Entries (1)
| P0C0L4 |
CO4A_HUMAN
Homo sapiens
Complement C4-A
|
PDB Structure
| PDB | 5JPM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Re-evaluation of low-resolution crystal structures via interactive molecular-dynamics flexible fitting (iMDFF): a case study in complement C4.
Acta Crystallogr D Struct Biol
|
