Research workbench

Wheat B-amylase, a clinically relevant food allergen

Analyse Wheat B-amylase, a clinically relevant food allergen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GER
Type: protein
Length: 488 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-amylase
EC: 3.2.1.2
UniProt: P93594
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-amylase (EC 3.2.1.2)	protein	488	39% helix, 12% strand	P93594

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	556	0.66	0.77	45	empty
2	70	0.35	0.77	19	empty
3	55	0.28	0.74	18	empty

Compared structures

6GER · Wheat b-amylase, a clinically relevant food allergen · the same entry in another collection · chain A against A, TM-score 1.00
P93594 · AlphaFold monomer V2.0 prediction for beta-amylase tri a 17 (P93594) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P93594
Elsewhere: RCSB PDB 6GER · PDBe 6GER · UniProt P93594

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