3lgv

X-ray diffraction
2.73Å resolution

H198P mutant of the DegS-deltaPDZ protease

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)
PDBe Complex ID:
PDB-CPX-142438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine endoprotease DegS Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 241 amino acids
Theoretical weight: 25.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEE3 (Residues: 27-256; Coverage: 65%)
Gene names: JW3204, b3235, degS, hhoB, htrH
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 71.54Å b: 133.565Å c: 230.272Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.27
Expression system: Escherichia coli