4hyg

X-ray diffraction
3.32Å resolution

Structure of a presenilin family intramembrane aspartate protease in C222 space group

Released:
Primary publication:
Structure of a presenilin family intramembrane aspartate protease.
Nature 493 56-61 (2013)
PMID: 23254940

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-107001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Signal peptide peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 301 amino acids
Theoretical weight: 31.88 KDa
Source organism: Methanoculleus marisnigri JR1
Expression system: Escherichia coli
UniProt:
  • Canonical: A3CWV0 (Residues: 1-301; Coverage: 100%)
Gene name: Memar_1924
Sequence domains: Signal-peptide peptidase, presenilin aspartyl protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C222
Unit cell:
a: 168.302Å b: 201.892Å c: 117.534Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.301 0.298 0.344
Expression system: Escherichia coli