Research workbench
Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions
Analyse Crystal structures of NLRP14 pyrin domain reveal a conformational switch… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N1L
- Type
- protein
- Length
- 95 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nacht, lrr and pyd domains-containing protein 14
- UniProt
- Q86W24
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nacht, lrr and pyd domains-containing protein 14 | protein | 95 | 78% helix, 0% strand | Q86W24 |
Compared structures
- 4N1L · Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism… · the same entry in another collection · chain A against A, TM-score 1.00
- Q86W24 · AlphaFold monomer V2.0 prediction for nacht, lrr and pyd domains- containing protein 14… · a predicted model of the same protein · chain A against A, TM-score 0.86
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q86W24
- Elsewhere: RCSB PDB 4N1L · PDBe 4N1L · UniProt Q86W24
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