Research workbench

AlphaFold monomer V2.0 prediction for hydrophobin-1 (P52754)

Analyse AlphaFold monomer V2.0 prediction for hydrophobin-1 (P52754) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P52754
Type: protein
Length: 97 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
Molecule: Hydrophobin-1
UniProt: P52754
Pockets: 1 · best druggability 0.28

Structure

1 distinct chain · 9% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrophobin-1	protein	97	9% helix, 26% strand	P52754

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	67	0.28	0.73	16	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2GVM · Crystal structure of hydrophobin HFBI with detergent · an experimental structure of the same protein · chain A against A, TM-score 0.70
2GVM · Crystal structure of hydrophobin hfbi with detergent · an experimental structure of the same protein · chain A against A, TM-score 0.70
2FZ6 · Crystal structure of hydrophobin HFBI · an experimental structure of the same protein · chain A against C, TM-score 0.70
2FZ6 · Crystal structure of hydrophobin hfbi · an experimental structure of the same protein · chain A against C, TM-score 0.70

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 P52754
Elsewhere: UniProt P52754 · AlphaFold DB P52754

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