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Beta-amylase from bacillus cereus var. mycoides complexed with maltopentaose

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

PDB: 1ITC
Type: protein
Length: 516 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-amylase
EC: 3.2.1.2
Ligands: GLC, CA, SO4
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-amylase (EC 3.2.1.2)	protein	516	38% helix, 19% strand	—

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 14 copies · chains A
CA · Calcium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
ACY · Acetic acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	338	0.75	0.86	48	GLC
2	74	0.32	0.74	14	empty
3	61	0.31	0.75	13	empty
4	57	0.27	0.74	21	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1ITC · Beta-Amylase from Bacillus cereus var. mycoides Complexed with Maltopentaose · 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
Elsewhere: RCSB PDB 1ITC · PDBe 1ITC

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