Function and Biology Details
Reactions catalysed:
Specificity similar to chymotrypsin C.
Hydrolysis of proteins, including elastin. Preferential cleavage Val-|- > Ala-|-.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-272417 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cathepsin G
Molecule details ›
Chains: C, F, I, L
Length: 223 amino acids
Theoretical weight: 25.4 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Length: 223 amino acids
Theoretical weight: 25.4 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P08311 (Residues: 21-243; Coverage: 94%)
Sequence domains: Trypsin
Protein map
Molecule details ›
Chains: B, E, H, K
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
Neutrophil elastase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P21
Expression system: Escherichia coli BL21(DE3)
