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

Analyse Crystal structure of glucosidase II alpha subunit (Tris-bound from) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DKX
Type: protein
Length: 925 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.4
Source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Molecule: Alpha glucosidase-like protein
UniProt: G0SG42
Ligands: CL
Pockets: 10 · best druggability 0.75

Structure

x-ray diffraction · resolution 1.4 · 1 distinct chain · 22% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha glucosidase-like protein	protein	925	22% helix, 29% strand	G0SG42

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

10 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	95	0.75	0.96	27	TRS
2	229	0.59	0.80	36	empty
3	109	0.47	0.80	18	empty
4	186	0.45	0.74	24	empty
5	64	0.43	0.82	22	empty

Compared structures

5DKX · Crystal structure of glucosidase II alpha subunit (tris-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 5DKX · PDBe 5DKX · UniProt G0SG42

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