1lcy

X-ray diffraction
2Å resolution

Crystal Structure of the Mitochondrial Serine Protease HtrA2

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:
monomeric (preferred)
homo trimer
PDBe Complex ID:
PDB-CPX-128931 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease HTRA2, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 35 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: R3
Unit cell:
a: 85.42Å b: 85.42Å c: 127.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.235 0.274
Expression system: Escherichia coli