Research workbench

AlphaFold monomer V2.0 prediction for lrr repeats and ubiquitin-like domain-containing protein AT2G30105 (P0C895)

Analyse AlphaFold monomer V2.0 prediction for lrr repeats and ubiquitin-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P0C895
Type: protein
Length: 374 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
Molecule: Lrr repeats and ubiquitin-like domain-containing protein AT2G30105
UniProt: P0C895
Pockets: 3 · best druggability 0.40

Structure

1 distinct chain · 24% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lrr repeats and ubiquitin-like domain-containing protein AT2G30105	protein	374	24% helix, 17% strand	P0C895

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.40	0.78	15	empty
2	56	0.30	0.76	17	empty
3	59	0.29	0.74	17	empty

Compared structures

2KD0 · NMR solution structure of O64736 protein from arabidopsis thaliana. northeast structural… · an experimental structure of the same protein · chain A against A, TM-score 0.20
2KD0 · NMR solution structure of O64736 protein from Arabidopsis thaliana. Northeast Structural… · an experimental structure of the same protein · chain A against A, TM-score 0.20

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 P0C895
Elsewhere: UniProt P0C895 · AlphaFold DB P0C895

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