Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I12, Bowman-Birk
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Bowman-Birk type proteinase inhibitor
- 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 domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133365 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1
Molecule details ›
Chain: A
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
Bowman-Birk type proteinase inhibitor
Molecule details ›
Chain: I
Length: 58 amino acids
Theoretical weight: 6.43 KDa
Source organism: Glycine max
UniProt:
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Length: 58 amino acids
Theoretical weight: 6.43 KDa
Source organism: Glycine max
UniProt:
- Canonical: P01055 (Residues: 45-102; Coverage: 64%)
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE BL-6A
Spacegroup:
P41212
