4rr0

X-ray diffraction
3.05Å resolution

re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE 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:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: P0AEE3 (Residues: 43-355; Coverage: 88%)
Gene names: JW3204, b3235, degS, hhoB, htrH
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 206.99Å b: 142.733Å c: 41.231Å
α: 90° β: 90.09° γ: 90°
R-values:
R R work R free
0.227 0.226 0.256
Expression system: Escherichia coli