Research workbench

Crystal structure of barley beta-amylase at atomic resolution

Analyse Crystal structure of barley beta-amylase at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XFR
Type: protein
Length: 487 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-amylase
EC: 3.2.1.2
UniProt: P16098
Pockets: 3 · best druggability 0.73

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-amylase (EC 3.2.1.2)	protein	487	38% helix, 12% strand	P16098

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

3 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	691	0.73	0.79	67	EDO
2	131	0.51	0.80	37	empty
3	58	0.36	0.79	19	empty

Compared structures

2XFR · Crystal structure of barley beta-amylase at atomic resolution · the same entry in another collection · chain A against A, TM-score 1.00
P16098 · AlphaFold monomer V2.0 prediction for beta-amylase (P16098) · 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 P16098
Elsewhere: RCSB PDB 2XFR · PDBe 2XFR · UniProt P16098

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.