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AlphaFold monomer V2.0 prediction for beta-1,4-xylanase (Q12603)

Analyse AlphaFold monomer V2.0 prediction for beta-1,4-xylanase (Q12603) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q12603
Type: protein
Length: 352 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x270E62591AbF98D9aE543aCe3b9CA0493e08E3E2
Molecule: Beta-1,4-xylanase
UniProt: Q12603
Pockets: 1 · best druggability 0.51

Structure

1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-1,4-xylanase	protein	352	41% helix, 17% strand	Q12603

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.51	0.78	28	empty

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 Q12603
Elsewhere: UniProt Q12603 · AlphaFold DB Q12603

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