MolNFT v1 · #18996 · protein

Crystal structure of soybean beta-amylase mutant (E178Y) with increased pH optimum at pH 5.4

1Q6E: “Crystal structure of soybean beta-amylase mutant (E178Y) with increased pH optimum at pH 5.4”. X-ray diffraction, 3 ligands (GLC, BGC, SO4), 5 pockets (best druggability 0.77). MolNFT v1 #18996 on GenesisL1: 3D structure, binding…

PDB: 1Q6E
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: 5 · 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

5 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	389	0.77	0.86	52	GLC, BGC
2	113	0.52	0.82	37	empty
3	135	0.43	0.76	21	empty
4	64	0.34	0.77	17	empty
5	51	0.26	0.74	13	empty

Compared structures

1Q6E · Crystal Structure of Soybean Beta-Amylase Mutant (E178Y) with Increased pH Optimum at pH… · 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 1Q6E · PDBe 1Q6E · UniProt Q42795

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