Research workbench

Beta-amylase from bacillus cereus var. mycoides in complex with maltose

Analyse Beta-amylase from bacillus cereus var. mycoides in complex with maltose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J0Z
Type: protein
Length: 2,064 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-amylase
EC: 3.2.1.2
UniProt: P36924
Ligands: GLC, BGC, CA
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Beta-amylase (EC 3.2.1.2)	protein	516	37% helix, 19% strand	P36924

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 10 copies · chains A, B, C, D
BGC · beta-D-glucopyranose · sugar · 6 copies · chains A, B, C, D
CA · Calcium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1109	0.80	0.81	128	BGC, GLC
2	894	0.76	0.80	110	empty
3	373	0.73	0.84	50	BGC, GLC
4	323	0.72	0.85	40	GLC
5	395	0.71	0.83	60	GLC

Interfaces

4 interfaces between chains.

A–B · 649 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 635 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 496 Å² buried · 1 hydrogen bond · protein-protein
B–D · 474 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1J0Z · Beta-amylase from Bacillus cereus var. mycoides in complex with maltose · the same entry in another collection · chain C against C, TM-score 1.00
P36924 · AlphaFold monomer V2.0 prediction for beta-amylase (P36924) · a predicted model of the same protein · 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 P36924
Elsewhere: RCSB PDB 1J0Z · PDBe 1J0Z · UniProt P36924

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