Function and Biology Details
Reaction catalysed:
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic pH-dependent serine endoprotease DegQ
Molecule details ›
Chains: A, B, C
Length: 245 amino acids
Theoretical weight: 25.66 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin-like peptidase domain
Structure domains: Trypsin-like serine proteases
Length: 245 amino acids
Theoretical weight: 25.66 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical:
P39099 (Residues: 28-264; Coverage: 55%)
Sequence domains: Trypsin-like peptidase domain
Structure domains: Trypsin-like serine proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU200
Spacegroup:
P31
Expression system: Escherichia coli
