Current Protein Identity:Q86W24 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
4N1J Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–100(100 aa) Fragment:UNP residues 1-100
Chain B 1–100(100 aa) Fragment:UNP residues 1-100
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.1 M HEPES pH 7.5, 2.6 M Ammonium sulfate and 2% PEG400, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.60 Å R-free 0.255
4N1J Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 1–100(100 aa) Fragment:UNP residues 1-100
Chain D 1–100(100 aa) Fragment:UNP residues 1-100
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.1 M HEPES pH 7.5, 2.6 M Ammonium sulfate and 2% PEG400, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.60 Å R-free 0.255
4N1J Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 3 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–100(100 aa) Fragment:UNP residues 1-100
Chain B 1–100(100 aa) Fragment:UNP residues 1-100
Chain C 1–100(100 aa) Fragment:UNP residues 1-100
Chain D 1–100(100 aa) Fragment:UNP residues 1-100
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.1 M HEPES pH 7.5, 2.6 M Ammonium sulfate and 2% PEG400, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.60 Å R-free 0.255
4N1K Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–100(100 aa) Fragment:UNP residues 1-100
Chain B 1–100(100 aa) Fragment:UNP residues 1-100
Mutation:D86V Mutation:D86V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.2 M Cesium chloride and 2.2 M Ammonium sulfate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.00 Å R-free 0.268
4N1K Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 1–100(100 aa) Fragment:UNP residues 1-100
Chain D 1–100(100 aa) Fragment:UNP residues 1-100
Mutation:D86V Mutation:D86V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.2 M Cesium chloride and 2.2 M Ammonium sulfate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.00 Å R-free 0.268
4N1K Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 3 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–100(100 aa) Fragment:UNP residues 1-100
Chain B 1–100(100 aa) Fragment:UNP residues 1-100
Chain C 1–100(100 aa) Fragment:UNP residues 1-100
Chain D 1–100(100 aa) Fragment:UNP residues 1-100
Mutation:D86V Mutation:D86V Mutation:D86V Mutation:D86V No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.2 M Cesium chloride and 2.2 M Ammonium sulfate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 3.00 Å R-free 0.268
4N1L Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions Deposited 2013-10-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–100(100 aa) Fragment:UNP residues 1-100
Mutation:L84R No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.2 M Ammonium acetate and 2.2 M Ammonium sulfate , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.99 Å R-free 0.222
9LN6 Structure of human NLRP14-UHRF1 complex Deposited 2025-01-20 Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–1093(1093 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.49 Å