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Structure of glycoside hydrolase family 32 from bifidobacterium adolescentis

Analyse Structure of glycoside hydrolase family 32 from bifidobacterium adolescentis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NOB
Type: protein
Length: 634 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-fructofuranosidase
UniProt: A1A323
Pockets: 8 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-fructofuranosidase	protein	634	6% helix, 50% strand	A1A323

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 4 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A

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

Pockets

8 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	382	0.61	0.77	34	EDO, PEG
2	85	0.61	0.89	33	empty
3	170	0.55	0.81	25	empty
4	60	0.52	0.87	24	empty
5	119	0.40	0.75	28	empty

Compared structures

6NOB · Structure of Glycoside Hydrolase family 32 from Bifidobacterium adolescentis · 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 A1A323
Elsewhere: RCSB PDB 6NOB · PDBe 6NOB · UniProt A1A323

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