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Crystal structure of a beta-glycosidase from bacteroides vulgatus

Analyse Crystal structure of a beta-glycosidase from bacteroides vulgatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GM8
Type: protein
Length: 770 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 2, candidate beta-glycosidase
EC: 3.2.1.-
UniProt: A6KXE5
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 2, candidate beta-glycosidase (EC 3.2.1.-)	protein	770	15% helix, 39% strand	A6KXE5

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.76	0.98	24	empty
2	417	0.69	0.81	32	empty
3	384	0.68	0.81	51	GOL
4	266	0.65	0.82	40	GOL
5	256	0.61	0.80	28	empty

Compared structures

3GM8 · Crystal structure of a beta-glycosidase from Bacteroides vulgatus · the same entry in another collection · 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 A6KXE5
Elsewhere: RCSB PDB 3GM8 · PDBe 3GM8 · UniProt A6KXE5

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