Research workbench

AlphaFold monomer V2.0 prediction for bacillolysin (P05806)

Analyse AlphaFold monomer V2.0 prediction for bacillolysin (P05806) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P05806
Type: protein
Length: 566 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7782F4817b37743d738e9aF842bf74bd50f2015E
Molecule: Bacillolysin
UniProt: P05806
Pockets: 5 · best druggability 0.71

Structure

1 distinct chain · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bacillolysin	protein	566	30% helix, 26% strand	P05806

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	509	0.71	0.80	75	empty
2	411	0.66	0.79	40	empty
3	261	0.55	0.77	43	empty
4	70	0.50	0.85	22	empty
5	104	0.35	0.74	20	empty

Compared structures

1ESP · Neutral protease mutant E144S · an experimental structure of the same protein · chain A against A, TM-score 0.56
1ESP · Neutral protease mutant E144S · an experimental structure of the same protein · chain A against A, TM-score 0.56
1NPC · The structure of neutral protease from bacillus cereus at 0.2-nm resolution · an experimental structure of the same protein · chain A against A, TM-score 0.56
1NPC · The structure of neutral protease from bacillus cereus at 0.2-nm resolution · an experimental structure of the same protein · chain A against A, TM-score 0.56

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 P05806
Elsewhere: UniProt P05806 · AlphaFold DB P05806

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