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Crystal structure of exo-inulinase from aspergillus awamori in spacegroup P21

Analyse Crystal structure of exo-inulinase from aspergillus awamori in spacegroup P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Y4W
Type: protein
Length: 517 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exo-inulinase
EC: 3.2.1.80
Ligands: NAG
Pockets: 4 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-inulinase (EC 3.2.1.80)	protein	517	3% helix, 48% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 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	200	0.54	0.78	28	empty
2	153	0.46	0.76	18	empty
3	106	0.46	0.79	17	GOL
4	53	0.29	0.75	19	empty

Modifications

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

Compared structures

1Y4W · Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P21 · 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
Elsewhere: RCSB PDB 1Y4W · PDBe 1Y4W

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