MolNFT v1 · #83944 · protein

Crystal structure of alpha-glucosidase in complex with glucose

3WY2: “Crystal structure of alpha-glucosidase in complex with glucose”. X-ray diffraction, 2 ligands (BGC, MG), 8 pockets (best druggability 0.77). MolNFT v1 #83944 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3WY2
Type: protein
Length: 1,070 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glucosidase
EC: 3.2.1.20
UniProt: H3K096
Ligands: BGC, MG
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alpha-glucosidase (EC 3.2.1.20)	protein	535	27% helix, 19% strand	H3K096

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · chains A
MG · Magnesium ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · 6 copies · chains A, B

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

Pockets

8 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	700	0.77	0.82	53	empty
2	342	0.72	0.84	54	BGC
3	316	0.71	0.84	51	GOL
4	58	0.46	0.84	14	empty
5	51	0.44	0.84	15	empty

Interfaces

1 interface between chains.

A–B · 596 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3WY2 · Crystal structure of alpha-glucosidase in complex with glucose · 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 H3K096
Elsewhere: RCSB PDB 3WY2 · PDBe 3WY2 · UniProt H3K096

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