Function and Biology Details
Reaction catalysed:
Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I11, ecotin
- Peptidase S1A, chymotrypsin family
- Proteinase inhibitor I11, ecotin, gammaproteobacteria
- Peptidase S1, PA clan, chymotrypsin-like fold
- Serine proteases, trypsin domain
- Ecotin, C-terminal
- Ecotin superfamily
- Serine proteases, trypsin family, serine active site
2 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Coagulation factor XIa light chain and Ecotin (preferred)
PDBe Complex ID:
PDB-CPX-137288 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Coagulation factor XIa light chain
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 26.83 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 238 amino acids
Theoretical weight: 26.83 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
- Canonical:
P03951 (Residues: 388-625; Coverage: 39%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ecotin
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RUH3R
Spacegroup:
P212121
Expression systems:
- Komagataella pastoris
- Escherichia coli BL21
