5tnz

X-ray diffraction
1.75Å resolution

HtrA2 S142D mutant

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

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-128934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease HTRA2, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 36.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43464 (Residues: 134-458; Coverage: 71%)
Gene names: HTRA2, OMI, PRSS25
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: R3
Unit cell:
a: 83.694Å b: 83.694Å c: 126.956Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.146 0.144 0.172
Expression system: Escherichia coli