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AlphaFold monomer V2.0 prediction for exo-1,4-beta-xylosidase xlnd (Q5BAS1)

Analyse AlphaFold monomer V2.0 prediction for exo-1,4-beta-xylosidase xlnd (Q5BAS1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q5BAS1
Type: protein
Length: 803 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x88DB42AFD1c918761d553B3c6CEc7ba83c6f79bC
Molecule: Exo-1,4-beta-xylosidase xlnd
UniProt: Q5BAS1
Pockets: 3 · best druggability 0.72

Structure

1 distinct chain · 29% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-1,4-beta-xylosidase xlnd	protein	803	29% helix, 19% strand	Q5BAS1

Pockets

3 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	379	0.72	0.83	44	empty
2	141	0.41	0.74	29	empty
3	54	0.26	0.73	14	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6Q7I · GH3 exo-beta-xylosidase (XlnD) · an experimental structure of the same protein · chain A against A, TM-score 0.96
6Q7I · GH3 exo-beta-xylosidase (xlnd) · an experimental structure of the same protein · chain A against A, TM-score 0.96
6Q7J · GH3 exo-beta-xylosidase (XlnD) in complex with xylobiose aziridine activity based probe · an experimental structure of the same protein · chain A against A, TM-score 0.96
6Q7J · GH3 exo-beta-xylosidase (xlnd) in complex with xylobiose aziridine activity based probe · an experimental structure of the same protein · chain A against A, TM-score 0.96

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 Q5BAS1
Elsewhere: UniProt Q5BAS1 · AlphaFold DB Q5BAS1

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