2NS5: Partitioning-defective 3 homolog

The conserved N-terminal domain of Par-3 adopts a novel PB1-like structure required for Par-3 oligomerization and apical membrane localization. Determined by solution NMR. Released 4 Sept 2007.

Method
Solution NMR
Organism
Rattus norvegicus
Chains
1
Atoms
679
Mol. weight
9.68 kDa
Released
4 Sept 2007

Explore 2NS5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2NS5 contains 2 α-helices and 5 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand18-2471
β-strand27-3371
α-helix40-5415
β-strand63-6971
β-strand75-7621
α-helix82-854
β-strand90-9891

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Partitioning-defective 3 homologAprotein85Rattus norvegicusQ9Z340 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2NS5_1 Partitioning-defective 3 homolog (chains A)
SEFKVTVCFGRTRVDVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGI
LDLDDILCDVADDKDRLVAVFDEQD

Primary citation

The Par-3 NTD adopts a PB1-like structure required for Par-3 oligomerization and membrane localization. Feng, W., Wu, H., Chan, L.-N. et al. EMBO J (2007) 26:2786-2796. DOI 10.1038/sj.emboj.7601702 · PubMed

Other PDB entries of the same protein (UniProt Q9Z340 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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