Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
Serine protease 1 and Alpha-1-antitrypsin (preferred)
PDBe Complex ID:
PDB-CPX-133324 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-1-antitrypsin
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 44.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Length: 394 amino acids
Theoretical weight: 44.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P01009 (Residues: 26-418; Coverage: 100%)
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Serine protease 1
Molecule details ›
Chain: B
Length: 243 amino acids
Theoretical weight: 25.43 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: 25.43 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:
APS BEAMLINE 22-ID
Spacegroup:
C2
Expression system: Escherichia coli
