MolNFT v1 · #262922 · protein

AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase nedd-4 (Q9VVI3)

Q9VVI3: “AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase nedd-4 (Q9VVI3)”. 11 pockets (best druggability 0.71). MolNFT v1 #262922 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: Q9VVI3
Type: protein
Length: 1,007 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xf87a97E0A4bB354D834857B14296240B167cbe70
Molecule: E3 ubiquitin-protein ligase nedd-4
UniProt: Q9VVI3
Pockets: 11 · best druggability 0.71

Structure

1 distinct chain · 24% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase nedd-4	protein	1007	24% helix, 16% strand	Q9VVI3

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	333	0.71	0.83	41	empty
2	705	0.65	0.74	57	empty
3	245	0.59	0.79	41	empty
4	142	0.53	0.81	24	empty
5	138	0.42	0.75	20	empty

Compared structures

2EZ5 · Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex · an experimental structure of the same protein · chain A against W, TM-score 0.04
2EZ5 · Solution structure of the DNEDD4 WW3* domain- comm lpsy peptide complex · an experimental structure of the same protein · chain A against W, TM-score 0.04

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 Q9VVI3
Elsewhere: UniProt Q9VVI3 · AlphaFold DB Q9VVI3

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