MolNFT v1 · #18998 · protein

Crystal structure of soybean beta-amylase mutant (N340T) with increased pH optimum

1Q6G: “Crystal structure of soybean beta-amylase mutant (N340T) with increased pH optimum”. X-ray diffraction, 3 ligands (GLC, BGC, SO4), 4 pockets (best druggability 0.77). MolNFT v1 #18998 on GenesisL1: 3D structure, binding sites and…

PDB: 1Q6G
Type: protein
Length: 490 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-amylase
EC: 3.2.1.2
UniProt: Q42795
Ligands: GLC, BGC, SO4
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-amylase (EC 3.2.1.2)	protein	490	40% helix, 12% strand	Q42795

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 3 copies · chains A
BGC · beta-D-glucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

4 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	402	0.77	0.86	47	GLC, BGC
2	132	0.56	0.83	40	empty
3	135	0.42	0.75	20	empty
4	70	0.37	0.78	20	empty

Compared structures

1Q6G · Crystal Structure of Soybean Beta-Amylase Mutant (N340T) with Increased pH Optimum · 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 Q42795
Elsewhere: RCSB PDB 1Q6G · PDBe 1Q6G · UniProt Q42795

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