Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I3, Kunitz legume
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Kunitz inhibitor STI-like superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Serine protease 1 and Kunitz-type inihibitor (preferred)
PDBe Complex ID:
PDB-CPX-133356 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1
Molecule details ›
Chains: A, B, C, D, E, F
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Kunitz-type inihibitor
Molecule details ›
Chains: G, H, I, J, K, L
Length: 169 amino acids
Theoretical weight: 18.71 KDa
Source organism: Bauhinia bauhinioides
Expression system: Escherichia coli
UniProt:
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Length: 169 amino acids
Theoretical weight: 18.71 KDa
Source organism: Bauhinia bauhinioides
Expression system: Escherichia coli
UniProt:
- Canonical: Q6VEQ7 (Residues: 19-181; Coverage: 93%)
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P64
Expression system: Escherichia coli
