MolNFT v1 · #127658 · protein

Crystal structure of the V72I mutant of the mouse alpha-dystroglycan N-terminal region

5N30: “Crystal structure of the V72I mutant of the mouse alpha-dystroglycan N-terminal region”. X-ray diffraction, 1 pocket (best druggability 0.48). MolNFT v1 #127658 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5N30
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dystroglycan
UniProt: Q62165
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dystroglycan	protein	229	19% helix, 36% strand	Q62165

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 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	197	0.48	0.75	27	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5N30 · Crystal structure of the V72I 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 5N30 · PDBe 5N30 · UniProt Q62165

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.