Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Serine protease 1 and Alpha-1-antitrypsin (preferred)
PDBe Complex ID:
PDB-CPX-133325 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Alpha-1-antitrypsin
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 37.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Length: 335 amino acids
Theoretical weight: 37.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P01009 (Residues: 48-382; Coverage: 85%)
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Short peptide from AAT
Serine protease 1
Molecule details ›
Chain: C
Length: 243 amino acids
Theoretical weight: 25.44 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 243 amino acids
Theoretical weight: 25.44 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
- Canonical: P00760 (Residues: 4-246; Coverage: 100%)
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:
SRS BEAMLINE PX9.6
Spacegroup:
C2221
Expression system: Escherichia coli
