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:
Neutrophil elastase and Protein map (preferred)
PDBe Complex ID:
PDB-CPX-140068 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Neutrophil elastase
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 23.32 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Length: 218 amino acids
Theoretical weight: 23.32 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P08246 (Residues: 30-247; Coverage: 91%)
Sequence domains: Trypsin
Protein map
Molecule details ›
Chains: C, D
Length: 100 amino acids
Theoretical weight: 11.02 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: MAP domain
Length: 100 amino acids
Theoretical weight: 11.02 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q99QS1 (Residues: 158-254; Coverage: 22%)
Sequence domains: MAP domain
Ligands and Environments
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
C2
Expression system: Escherichia coli BL21(DE3)
