MolNFT v1 · #64258 · protein

Dishevelled PDZ domain homodimer

3FY5 · Segment polarity protein dishevelled homolog dvl- 2: “Dishevelled PDZ domain homodimer”. X-ray diffraction, 1 pocket (best druggability 0.36). MolNFT v1 #64258 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3FY5
Type: protein
Length: 176 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Segment polarity protein dishevelled homolog dvl- 2
UniProt: P51142
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Segment polarity protein dishevelled homolog dvl- 2	protein	91	20% helix, 36% strand	P51142
B	Segment polarity protein dishevelled homolog dvl- 2	protein	85	14% helix, 33% strand	P51142

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	50	0.36	0.80	16	empty

Interfaces

1 interface between chains.

A–B · 628 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3FY5 · Dishevelled PDZ domain homodimer · the same entry in another collection · chain A against A, TM-score 1.00
P51142 · AlphaFold monomer V2.0 prediction for segment polarity protein dishevelled homolog dvl-2… · a predicted model of the same protein · chain B against A, TM-score 0.94

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 P51142
Elsewhere: RCSB PDB 3FY5 · PDBe 3FY5 · UniProt P51142

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