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Crystal structure of the D109N mutant of the mouse alpha-dystroglycan N-terminal region

Analyse Crystal structure of the D109N mutant of the mouse alpha-dystroglycan… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5N4H
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dystroglycan
UniProt: Q62165
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dystroglycan	protein	231	19% helix, 35% strand	Q62165

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.42	0.75	29	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5N4H · Crystal structure of the D109N mutant of the mouse alpha-Dystroglycan N-terminal region · the same entry in another collection · chain A against A, TM-score 1.00
Q62165 · AlphaFold monomer V2.0 prediction for dystroglycan (Q62165) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q62165
Elsewhere: RCSB PDB 5N4H · PDBe 5N4H · UniProt Q62165

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