Current Protein Identity:Q86W24
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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 |