Research workbench

Structural basis of the recognition of the dishevelled dep domain in the wnt signaling pathway

Analyse Structural basis of the recognition of the dishevelled dep domain in the wnt… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FSH
Type: protein
Length: 94 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dishevelled-1
UniProt: P51141
Pockets: 1 · best druggability 0.32

Structure

solution nmr · 1 distinct chain · 39% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dishevelled-1	protein	94	39% helix, 11% strand	P51141

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	51	0.32	0.77	13	empty

Compared structures

1FSH · Structural basis of the recognition of the dishevelled dep domain in the wnt signaling… · the same entry in another collection · chain A against A, TM-score 1.00
P51141 · AlphaFold monomer V2.0 prediction for segment polarity protein dishevelled homolog dvl-1… · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P51141
Elsewhere: RCSB PDB 1FSH · PDBe 1FSH · UniProt P51141

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