4a8c

Electron Microscopy
7.5Å resolution

Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide

Released:
Source organism: Escherichia coli K-12
Related structures: EMD-1983

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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: 436 amino acids
Theoretical weight: 45.54 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39099 (Residues: 28-455; Coverage: 100%)
Gene names: JW3203, b3234, degQ, hhoA
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 7.5Å
Relevant EMDB volumes: EMD-1983
Expression system: Escherichia coli BL21(DE3)