4n1j

X-ray diffraction
2.6Å resolution

Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-183221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NACHT, LRR and PYD domains-containing protein 14 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 105 amino acids
Theoretical weight: 12.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86W24 (Residues: 1-100; Coverage: 9%)
Gene names: NALP14, NLRP14, NOD5
Sequence domains: PAAD/DAPIN/Pyrin domain
Structure domains: Death Domain, Fas

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P63
Unit cell:
a: 89.61Å b: 89.61Å c: 107.871Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.209 0.255
Expression system: Escherichia coli BL21(DE3)