Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Trypsin Inhibitor-like, cysteine rich domain
- Serine protease inhibitor-like superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-133453 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsin-like elastase family member 1
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
UniProt:
- Canonical:
P00772 (Residues: 27-266; Coverage: 96%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Chymotrypsin/elastase isoinhibitor 1
Molecule details ›
Chains: C, D
Length: 61 amino acids
Theoretical weight: 6.6 KDa
Source organism: Ascaris suum
UniProt:
Structure domains: Laminin
Length: 61 amino acids
Theoretical weight: 6.6 KDa
Source organism: Ascaris suum
UniProt:
- Canonical: P07851 (Residues: 1-61; Coverage: 97%)
Structure domains: Laminin
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SIEMENS
Spacegroup:
P3221
