CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
4 | Few Secondary Structures |
|
4.10 | Irregular |
|
4.10.740 | Coagulation Factor IX |
|
4.10.740.10 | Coagulation Factor IX |
Domain Context
CATH Clusters
| Superfamily | Coagulation Factor IX |
| Functional Family |
Enzyme Information
| 3.4.21.6 |
Coagulation factor Xa.
based on mapping to UniProt P00743
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
-!- A blood coagulation factor formed from the proenzyme factor X by limited proteolysis. -!- Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds. -!- The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca(2+) and phospholipids. -!- Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va. -!- Belongs to peptidase family S1.
|
UniProtKB Entries (1)
| P00743 |
FA10_BOVIN
Bos taurus
Coagulation factor X
|
PDB Structure
| PDB | 1WHE |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
Biochemistry
|
