Research workbench

AlphaFold monomer V2.0 prediction for beta-2-syntrophin (Q13425)

Analyse AlphaFold monomer V2.0 prediction for beta-2-syntrophin (Q13425) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q13425
Type: protein
Length: 540 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
Molecule: Beta-2-syntrophin
UniProt: Q13425
Pockets: 8 · best druggability 0.63

Structure

1 distinct chain · 20% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-2-syntrophin	protein	540	20% helix, 34% strand	Q13425

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	333	0.63	0.79	46	empty
2	345	0.62	0.78	39	empty
3	136	0.41	0.75	16	empty
4	86	0.35	0.74	13	empty
5	85	0.34	0.74	14	empty

Compared structures

2VRF · Crystal structure of the human beta-2-syntrophin PDZ domain · an experimental structure of the same protein · chain A against A, TM-score 0.17
2VRF · Crystal structure of the human beta-2-syntrophin PDZ domain · an experimental structure of the same protein · chain A against A, TM-score 0.17

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 Q13425
Elsewhere: UniProt Q13425 · AlphaFold DB Q13425

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