MolNFT v1 · #83943 · protein

Crystal structure of alpha-glucosidase

3WY1: “Crystal structure of alpha-glucosidase”. X-ray diffraction, 2 ligands (PRU, MG), 7 pockets (best druggability 0.77). MolNFT v1 #83943 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3WY1
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: PRU, MG
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alpha-glucosidase (EC 3.2.1.20)	protein	535	28% helix, 19% strand	H3K096

Ligands and binding sites

PRU · (3R,5R,7R)-octane-1,3,5,7-tetracarboxylic acid · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	801	0.77	0.81	58	empty
2	348	0.73	0.85	52	PRU
3	330	0.73	0.85	50	PRU
4	65	0.57	0.88	15	empty
5	131	0.42	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 560 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3WY1 · Crystal structure of 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
Every structure of UniProt H3K096
Elsewhere: RCSB PDB 3WY1 · PDBe 3WY1 · UniProt H3K096

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