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Beta-fructofuranosidase from bifidobacterium longum

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

PDB: 3PIG
Type: protein
Length: 1,049 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-fructofuranosidase
EC: 3.2.1.26
UniProt: A2TLS9
Ligands: CL
Pockets: 12 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-fructofuranosidase (EC 3.2.1.26)	protein	523	8% helix, 51% strand	A2TLS9
B	Beta-fructofuranosidase (EC 3.2.1.26)	protein	526	7% helix, 50% strand	A2TLS9

Ligands and binding sites

CL · Chloride ion · ion · 6 copies · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	229	0.61	0.81	45	empty
2	207	0.60	0.81	37	empty
3	232	0.58	0.79	31	empty
4	216	0.56	0.78	25	empty
5	55	0.44	0.84	21	empty

Interfaces

1 interface between chains.

A–B · 1404 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

3PIG · beta-fructofuranosidase from Bifidobacterium longum · 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 A2TLS9
Elsewhere: RCSB PDB 3PIG · PDBe 3PIG · UniProt A2TLS9

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