5fht

X-ray diffraction
1.95Å resolution

HtrA2 protease mutant V226K

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:
monomeric (preferred)
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: 334 amino acids
Theoretical weight: 36.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O43464 (Residues: 134-458; Coverage: 71%)
Gene names: HTRA2, OMI, PRSS25
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: R3
Unit cell:
a: 86.01Å b: 86.01Å c: 126.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.228
Expression system: Escherichia coli BL21(DE3)