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Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose

Analyse Crystal structure of exo-inulinase from Aspergillus awamori complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Y9G
Type: protein
Length: 517 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.87
Source: Aspergillus awamori
Molecule: exo-inulinase
EC: 3.2.1.80
Ligands: NAG, FRU
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · resolution 1.87 · 1 distinct chain · 2% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	exo-inulinase (EC 3.2.1.80)	protein	517	2% helix, 49% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
FRU · beta-D-fructofuranose · sugar · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	209	0.56	0.79	35	empty
2	152	0.46	0.76	17	empty
3	103	0.45	0.79	18	FRU

Modifications

Observed in the structure: 4 glycan (N-glycosylation).

Compared structures

1Y9G · Crystal structure of exo-inulinase from aspergillus awamori complexed with fructose · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1Y9G · PDBe 1Y9G

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