MolNFT v1 · #148538 · protein

Crystal structure of barley beta-amylase complexed with 3-deoxy-3- fluoro-maltose

6F9L: “Crystal structure of barley beta-amylase complexed with 3-deoxy-3- fluoro-maltose”. X-ray diffraction, 3 ligands (TUP, GLC, CL), 3 pockets (best druggability 0.71). MolNFT v1 #148538 on GenesisL1: 3D structure, binding sites and…

PDB: 6F9L
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: TUP, GLC, CL
Pockets: 3 · best druggability 0.71

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

TUP · 3-deoxy-3-fluoro-alpha-D-glucopyranose · 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

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	598	0.71	0.79	54	TUP, GLC
2	120	0.51	0.81	40	empty
3	54	0.31	0.77	17	empty

Compared structures

6F9L · Crystal structure of Barley Beta-Amylase complexed with 3-Deoxy-3-fluoro-maltose · 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 6F9L · PDBe 6F9L · UniProt A8CFR3

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