Research workbench

AlphaFold monomer V2.0 prediction for D-xylonate dehydratase (Q9A9Z2)

Analyse AlphaFold monomer V2.0 prediction for D-xylonate dehydratase (Q9A9Z2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9A9Z2
Type: protein
Length: 595 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xed981C7Bde83976797b0E4fB64b4974D133Bd529
Molecule: D-xylonate dehydratase
UniProt: Q9A9Z2
Pockets: 6 · best druggability 0.58

Structure

1 distinct chain · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-xylonate dehydratase	protein	595	38% helix, 15% strand	Q9A9Z2

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	309	0.58	0.77	45	empty
2	130	0.50	0.80	32	empty
3	69	0.40	0.79	15	empty
4	69	0.35	0.76	12	empty
5	52	0.29	0.75	14	empty

Compared structures

5OYN · Crystal structure of D-xylonate dehydratase in holo-form · an experimental structure of the same protein · chain A against B, TM-score 0.99
5OYN · Crystal structure of D-xylonate dehydratase in holo-form · an experimental structure of the same protein · chain A against A, TM-score 0.99

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 Q9A9Z2
Elsewhere: UniProt Q9A9Z2 · AlphaFold DB Q9A9Z2

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