5E11: Ligand of Numb protein X 2

Second PDZ domain of Ligand of Numb protein X 2 by Laue crystallography (no electric field). Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Dec 2016.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 929
Mol. weight: 10.31 kDa
Released: 7 Dec 2016

Explore 5E11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5E11 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

>5E11_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
5E21 1.01 Å, PDZ2 of LNX2 at 277K,single conformer model
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…
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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