Function and Biology Details
Reaction catalysed:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I12, Bowman-Birk
- Serine proteases, trypsin domain
- Peptidase S1A, chymotrypsin family
- 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 analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133431 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A
Molecule details ›
Chain: A
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00766 (Residues: 1-245; Coverage: 100%)
Structure domains: Trypsin-like serine proteases
Bowman-Birk type proteinase inhibitor
Molecule details ›
Chain: B
Length: 71 amino acids
Theoretical weight: 7.9 KDa
Source organism: Glycine max
Expression system: Not provided
UniProt:
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Length: 71 amino acids
Theoretical weight: 7.9 KDa
Source organism: Glycine max
Expression system: Not provided
UniProt:
- Canonical: P01055 (Residues: 40-110; Coverage: 78%)
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
RIGAKU MICROMAX-007 HF
Spacegroup:
P21212
Expression system: Not provided
