3mh7

X-ray diffraction
2.96Å resolution

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero 72-mer (preferred)
PDBe Complex ID:
PDB-CPX-142923 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Periplasmic serine endoprotease DegP Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 48.58 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0V0 (Residues: 27-474; Coverage: 100%)
Gene names: JW0157, b0161, degP, htrA, ptd
Sequence domains:
Structure domains:
5-mer peptide Chains: B, C
Molecule details ›
Chains: B, C
Length: 5 amino acids
Theoretical weight: 444 Da
Source organism: Escherichia coli K-12
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: F432
Unit cell:
a: 253.929Å b: 253.929Å c: 253.929Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.249
Expression system: Escherichia coli