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Beta-D-glucan exohydrolase from barley

Analyse Beta-D-glucan exohydrolase from barley in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EX1
Type: protein
Length: 602 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (beta-D-glucan exohydrolase isoenzyme EXO1)
EC: 3.2.1.58
Ligands: NAG, MAN, FCA, GLC
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (beta-D-glucan exohydrolase isoenzyme EXO1) (EC 3.2.1.58)	protein	602	38% helix, 12% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
FCA · alpha-D-fucopyranose · sugar · chains A
GLC · alpha-D-glucopyranose · sugar · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.48	0.83	19	GLC
2	68	0.34	0.76	17	empty

Modifications

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

Compared structures

1EX1 · Beta-D-glucan exohydrolase from barley · 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 1EX1 · PDBe 1EX1

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