Research workbench
The conserved N-terminal domain of par-3 adopts a novel PB1-like structure required for par-3 oligomerization and apical membrane localization
Analyse The conserved N-terminal domain of par-3 adopts a novel PB1-like structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NS5
- Type
- protein
- Length
- 85 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Partitioning-defective 3 homolog
- UniProt
- Q9Z340
Structure
solution nmr · 1 distinct chain · 22% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Partitioning-defective 3 homolog | protein | 85 | 22% helix, 38% strand | Q9Z340 |
Compared structures
- 2NS5 · The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Z340 · AlphaFold monomer V2.0 prediction for partitioning defective 3 homolog (Q9Z340) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q9Z340
- Elsewhere: RCSB PDB 2NS5 · PDBe 2NS5 · UniProt Q9Z340
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