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Sugar beet alpha-glucosidase

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

PDB: 3W38
Type: protein
Length: 826 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase
EC: 3.2.1.20
Ligands: NAG, FUC, SO4
Pockets: 6 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-glucosidase (EC 3.2.1.20)	protein	826	21% helix, 33% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
FUC · alpha-L-fucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.54	0.85	22	SO4
2	100	0.52	0.82	23	empty
3	59	0.35	0.79	15	SO4
4	54	0.28	0.74	15	empty
5	67	0.28	0.73	17	empty

Modifications

Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).

Compared structures

3W38 · Sugar beet alpha-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
Elsewhere: RCSB PDB 3W38 · PDBe 3W38

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