5E21: PDZ2 of LNX2 at 277K,single conformer model

PDZ2 of LNX2 at 277K,single conformer model. Determined by X-ray diffraction at 1.01 Å resolution. Released 7 Dec 2016.

Method: X-ray diffraction
Resolution: 1.01 Å
Organism: Homo sapiens
Chains: 1
Atoms: 824
Mol. weight: 10.31 kDa
Released: 7 Dec 2016

Explore 5E21 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5E21 contains 2 α-helices and 6 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, 6 β-strands

Element	Residues	Length	Sheet
β-strand	335-343	9	1
β-strand	353-356	4	1
β-strand	364-369	6	1
α-helix	374-378	5
β-strand	386-390	5	1
β-strand	393-394	2	1
α-helix	400-408	9
β-strand	413-421	9	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ligand of Numb protein X 2	A	protein	95	Homo sapiens	Q8N448 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5E21_1 Ligand of Numb protein X 2 (chains A)
SMEILQVALHKRDSGEQLGIKLVRRTDEPGVFILDLLEGGLAAQDGRLSSNDRVLAINGH
DLKYGTPELAAQIIQASGERVNLTIARPGKPEIEL

Primary citation

Electric-field-stimulated protein mechanics. Hekstra, D.R., White, K.I., Socolich, M.A. et al. Nature (2016) 540:400-405. DOI 10.1038/nature20571 · PubMed

Other PDB entries of the same protein (UniProt Q8N448 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5E1Y 1.01 Å, PDZ2 of LNX2 at 277K, model with alternate conformations
2VWR 1.3 Å, Crystal structure of the second pdz domain of numb-binding protein 2
5E22 1.8 Å, The second PDZ domain of Ligand of Numb protein X 2 in the presence of an electric field…
5E11 1.8 Å, Second PDZ domain of Ligand of Numb protein X 2 by Laue crystallography (no electric…
5DIN 1.86 Å, Structural Basis for the Indispensable Role of a Unique Zinc Finger Motif in LNX2…
7QCT 3.2 Å, PDZ2 of LNX2 with SARS-CoV-2_E PBM complex

Browse structure collections

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