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Crystal structure of barley beta-amylase complexed with 4-S-alpha-D- glucopyranosyl-(1,4-dideoxy-4-thio-nojirimycin)

Analyse Crystal structure of barley beta-amylase complexed with 4-S-alpha-D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F9H
Type: protein
Length: 485 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-amylase
EC: 3.2.1.2
UniProt: A8CFR3
Ligands: SGJ, GLC, CL
Pockets: 2 · best druggability 0.76

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	485	38% helix, 12% strand	A8CFR3

Ligands and binding sites

SGJ · 1,4-dideoxy-4-thio-nojirimycin · ligand · chains A
GLC · alpha-D-glucopyranose · sugar · chains A
CL · Chloride ion · ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	371	0.76	0.86	50	SGJ, GLC
2	134	0.55	0.82	37	empty

Compared structures

6F9H · Crystal structure of Barley Beta-Amylase complexed with… · 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 A8CFR3
Elsewhere: RCSB PDB 6F9H · PDBe 6F9H · UniProt A8CFR3

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