Research workbench

AlphaFold monomer V2.0 prediction for protein scalloped (P30052)

Analyse AlphaFold monomer V2.0 prediction for protein scalloped (P30052) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P30052
Type: protein
Length: 440 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x20eE38DD6CF7B82Bed838E99B58F03211C6277E8
Molecule: Protein scalloped
UniProt: P30052
Pockets: 7 · best druggability 0.80

Structure

1 distinct chain · 20% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein scalloped	protein	440	20% helix, 25% strand	P30052

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	218	0.80	0.93	38	empty
2	137	0.50	0.79	22	empty
3	103	0.38	0.75	21	empty
4	73	0.31	0.74	16	empty
5	81	0.29	0.72	13	empty

Compared structures

6Y20 · Crystal structure of protein scalloped (222-440) bound to protein vestigial (298-337) · an experimental structure of the same protein · chain A against A, TM-score 0.48
6Y20 · Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337) · an experimental structure of the same protein · chain A against A, TM-score 0.48
8A8Q · Crystal structure of Protein Scalloped in complex with YAP peptide · an experimental structure of the same protein · chain A against A, TM-score 0.46

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 P30052
Elsewhere: UniProt P30052 · AlphaFold DB P30052

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