Function and Biology Details
Reaction catalysed:
Degradation of blood coagulation factors Va and VIIIa.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- EGF-like domain
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- EGF-type aspartate/asparagine hydroxylation site
- EGF-like calcium-binding, conserved site
- EGF-like calcium-binding domain
- Serine proteases, trypsin family, serine active site
2 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Active Protein C complex (preferred)
PDBe Complex ID:
PDB-CPX-137386 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vitamin K-dependent protein C heavy chain
Molecule details ›
Chain: C
Length: 250 amino acids
Theoretical weight: 28.09 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 250 amino acids
Theoretical weight: 28.09 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P04070 (Residues: 212-461; Coverage: 56%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Vitamin K-dependent protein C light chain
Molecule details ›
Chain: L
Length: 114 amino acids
Theoretical weight: 12.73 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
Length: 114 amino acids
Theoretical weight: 12.73 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P04070 (Residues: 84-197; Coverage: 26%)
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
