Research workbench

Beta-glucosidase B from bacillus polymyxa complexed with glucose

Analyse Beta-glucosidase B from bacillus polymyxa complexed with glucose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O9T
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucosidase B
EC: 3.2.1.21
UniProt: P22505
Ligands: BGC
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosidase B (EC 3.2.1.21)	protein	445	44% helix, 17% strand	P22505

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	535	0.74	0.81	49	BGC

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2O9T · beta-glucosidase B from Bacillus polymyxa complexed with glucose · the same entry in another collection · chain A against A, TM-score 1.00
P22505 · AlphaFold monomer V2.0 prediction for beta-glucosidase B (P22505) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P22505
Elsewhere: RCSB PDB 2O9T · PDBe 2O9T · UniProt P22505

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