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Expression, characterization and crystal structure of a novel beta- glucosidase from paenibacillus barengoltzii

Analyse Expression, characterization and crystal structure of a novel beta- glucosidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WVP
Type: protein
Length: 924 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucosidase
EC: 3.2.1.21
UniProt: A0A1P8VKA0
Ligands: BMA
Pockets: 7 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosidase (EC 3.2.1.21)	protein	924	26% helix, 27% strand	A0A1P8VKA0

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · chains A

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

Pockets

7 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	214	0.71	0.87	28	empty
2	494	0.64	0.77	67	empty
3	100	0.47	0.80	18	BMA
4	159	0.43	0.75	25	empty
5	85	0.42	0.79	23	empty

Compared structures

5WVP · Expression, characterization and crystal structure of a novel beta-glucosidase from… · 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 A0A1P8VKA0
Elsewhere: RCSB PDB 5WVP · PDBe 5WVP · UniProt A0A1P8VKA0

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