Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I12, Bowman-Birk
- Bowman-Birk type proteinase inhibitor
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133353 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bowman-Birk type bran trypsin inhibitor
Molecule details ›
Chain: B
Length: 133 amino acids
Theoretical weight: 15.1 KDa
Source organism: Oryza sativa Japonica Group
UniProt:
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Length: 133 amino acids
Theoretical weight: 15.1 KDa
Source organism: Oryza sativa Japonica Group
UniProt:
- Canonical:
Q0JR25 (Residues: 119-251; Coverage: 57%)
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Serine protease 1
Molecule details ›
Chain: T
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
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL12B2
Spacegroup:
P43212
