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AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase B (P26515)

Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase B (P26515) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P26515
Type: protein
Length: 335 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
Molecule: Endo-1,4-beta-xylanase B
UniProt: P26515
Pockets: 2 · best druggability 0.51

Structure

1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase B	protein	335	6% helix, 53% strand	P26515

Pockets

2 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	194	0.51	0.77	30	empty
2	121	0.37	0.73	23	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5EJ3 · Crystal structure of XlnB2 · an experimental structure of the same protein · chain A against B, TM-score 0.57
5EJ3 · Crystal structure of XLNB2 · an experimental structure of the same protein · chain A against A, TM-score 0.57

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 P26515
Elsewhere: UniProt P26515 · AlphaFold DB P26515

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