Research workbench

Beta-glucosidase

Analyse Beta-glucosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F1N
Type: protein
Length: 1,004 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-galactosidase
UniProt: A0A256XQM7
Ligands: MG
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-galactosidase	protein	502	41% helix, 18% strand	A0A256XQM7
B	Beta-galactosidase	protein	502	40% helix, 19% strand	A0A256XQM7

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	550	0.79	0.85	48	empty
2	738	0.77	0.82	86	empty
3	670	0.76	0.81	52	empty
4	121	0.39	0.75	22	empty
5	60	0.35	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 719 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7F1N · Beta-Glucosidase · 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 A0A256XQM7
Elsewhere: RCSB PDB 7F1N · PDBe 7F1N · UniProt A0A256XQM7

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