MolNFT v1 · #116679 · protein

Crystal structure of glucosidase II alpha subunit (ALPHA3-GLC2-bound from)

5DKZ · Alpha glucosidase-like protein: “Crystal structure of glucosidase II alpha subunit (ALPHA3-GLC2-bound from)”. X-ray diffraction, 1 ligand (GLC), 11 pockets (best druggability 0.67). MolNFT v1 #116679 on GenesisL1: 3D structure…

PDB: 5DKZ
Type: protein
Length: 921 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha glucosidase-like protein
UniProt: G0SG42
Ligands: GLC
Pockets: 11 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha glucosidase-like protein	protein	921	22% helix, 29% strand	G0SG42

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.67	0.97	28	empty
2	134	0.61	0.84	22	GLC
3	245	0.60	0.80	38	empty
4	118	0.49	0.80	20	empty
5	153	0.42	0.74	19	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5DKZ · Crystal structure of glucosidase II alpha subunit (alpha3-Glc2-bound from) · 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 G0SG42
Elsewhere: RCSB PDB 5DKZ · PDBe 5DKZ · UniProt G0SG42

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