MolNFT v1 · #19594 · protein

Beta-glucosidase from bacillus circulans sp. alkalophilus

1QOX: “Beta-glucosidase from bacillus circulans sp. alkalophilus”. X-ray diffraction, 20 pockets (best druggability 0.76). MolNFT v1 #19594 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1QOX
Type: protein
Length: 7,184 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucosidase
EC: 3.2.1.21
UniProt: Q03506
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Beta-glucosidase (EC 3.2.1.21)	protein	449	42% helix, 17% strand	Q03506

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	951	0.76	0.79	81	empty
2	297	0.72	0.85	36	empty
3	313	0.72	0.85	32	empty
4	307	0.72	0.84	33	empty
5	317	0.71	0.84	31	empty

Interfaces

30 interfaces between chains.

K–O · 1259 Å² buried · 20 hydrogen bonds · protein-protein
J–P · 1255 Å² buried · 20 hydrogen bonds · protein-protein
I–M · 1249 Å² buried · 18 hydrogen bonds · protein-protein
A–E · 1249 Å² buried · 17 hydrogen bonds · protein-protein
C–G · 1244 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1QOX · Beta-glucosidase from Bacillus circulans sp. alkalophilus · the same entry in another collection · chain K against K, 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 Q03506
Elsewhere: RCSB PDB 1QOX · PDBe 1QOX · UniProt Q03506

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