Function and Biology Details
Reaction catalysed:
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Coagulation factor IXa light chain
Molecule details ›
Chain: E
Length: 58 amino acids
Theoretical weight: 6.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
Length: 58 amino acids
Theoretical weight: 6.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P00740 (Residues: 134-191; Coverage: 13%)
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
Coagulation factor IXa heavy chain
Molecule details ›
Chain: S
Length: 235 amino acids
Theoretical weight: 26.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 235 amino acids
Theoretical weight: 26.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P00740 (Residues: 227-461; Coverage: 54%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
