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Crystal structure of human alpha-dystroglycan

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

PDB: 5LLK
Type: protein
Length: 226 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dystroglycan
UniProt: Q14118
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dystroglycan	protein	226	20% helix, 37% strand	Q14118

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	251	0.53	0.76	28	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5LLK · Crystal structure of human alpha-dystroglycan · the same entry in another collection · chain A against A, TM-score 1.00
Q14118 · AlphaFold monomer V2.0 prediction for dystroglycan (Q14118) · 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 Q14118
Elsewhere: RCSB PDB 5LLK · PDBe 5LLK · UniProt Q14118

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