1soz

X-ray diffraction
2.4Å resolution

Crystal Structure of DegS protease in complex with an activating peptide

Released:

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine endoprotease DegS Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 314 amino acids
Theoretical weight: 33.24 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEE3 (Residues: 43-355; Coverage: 88%)
Gene names: JW3204, b3235, degS, hhoB, htrH
Sequence domains:
Structure domains:
activating peptide Chains: D, E
Molecule details ›
Chains: D, E
Length: 10 amino acids
Theoretical weight: 1.23 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 205.984Å b: 142.71Å c: 41.167Å
α: 90° β: 89.24° γ: 90°
R-values:
R R work R free
0.214 0.213 0.272
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided