7vge

X-ray diffraction
4Å resolution

Structure of the PDZ deleted variant of HtrA2 protease (S306A)

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo trimer
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-128932 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Serine protease HTRA2, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 203 amino acids
Theoretical weight: 21.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43464 (Residues: 140-342; Coverage: 44%)
Gene names: HTRA2, OMI, PRSS25
Sequence domains: Trypsin-like peptidase domain
Serine protease HTRA2, mitochondrial Chains: D, F
Molecule details ›
Chains: D, F
Length: 202 amino acids
Theoretical weight: 21.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43464 (Residues: 140-341; Coverage: 44%)
Gene names: HTRA2, OMI, PRSS25
Sequence domains: Trypsin-like peptidase domain
Serine protease HTRA2, mitochondrial Chain: E
Molecule details ›
Chain: E
Length: 201 amino acids
Theoretical weight: 21.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43464 (Residues: 140-340; Coverage: 44%)
Gene names: HTRA2, OMI, PRSS25
Sequence domains: Trypsin-like peptidase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 82.88Å b: 82.88Å c: 395.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.265 0.336
Expression system: Escherichia coli