3stj

X-ray diffraction
2.6Å resolution

Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli

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

Assemblies composition:
hetero heptamer
hetero hexamer (preferred)
hetero 25-mer
PDBe Complex ID:
PDB-CPX-153830 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Periplasmic pH-dependent serine endoprotease DegQ Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 345 amino acids
Theoretical weight: 36.01 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P39099 (Residues: 28-364; Coverage: 79%)
Gene names: JW3203, b3234, degQ, hhoA
Sequence domains:
Structure domains:
peptide (UNK) Chains: M, N, O, P, Q, R, S, T, U, V, W, X, Z
Molecule details ›
Chains: M, N, O, P, Q, R, S, T, U, V, W, X, Z
Length: 7 amino acids
Theoretical weight: 614 Da
Source organism: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P31
Unit cell:
a: 115.316Å b: 115.316Å c: 287.419Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.184 0.212
Expression system: Escherichia coli