› 5m3o

X-ray diffraction
1.7Å resolution

HTRA2 A141S mutant structure

Released:
DOI: 10.2210/pdb5m3o/pdb
PDB entry 5m3o coloured by chain, front view.
PDB entry 5m3o coloured by chain, side view.
PDB entry 5m3o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.
Merski M, Moreira C, Abreu RM, Ramos MJ, Fernandes PA, Martins LM, Pereira PJB, Macedo-Ribeiro S
Cell Death Dis 8 e3119 (2017)
PMID: 29022916

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
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: 334 amino acids
Theoretical weight: 36.26 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

1 bound ligand:
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: R3
Unit cell:
a: 84.291Å b: 84.291Å c: 127.978Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.2
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
1 more

2 mentions without citation

Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.
Merski et al. (2017)
1 more