Function and Biology Details
Reaction catalysed:
Hydrolysis of proteins, including elastin. Preferential cleavage Val-|- > Ala-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102021 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Neutrophil elastase
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 23.32 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 218 amino acids
Theoretical weight: 23.32 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P08246 (Residues: 30-247; Coverage: 91%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
MAP domain-containing protein
Molecule details ›
Chain: B
Length: 114 amino acids
Theoretical weight: 12.72 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: MAP domain
Structure domains: Ubiquitin-like (UB roll)
Length: 114 amino acids
Theoretical weight: 12.72 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: A0A0H3K0M1 (Residues: 43-141; Coverage: 89%)
Sequence domains: MAP domain
Structure domains: Ubiquitin-like (UB roll)
Ligands and Environments
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P61
Expression system: Escherichia coli BL21(DE3)
