Research workbench

Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from bacillus licheniformis

Analyse Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3D6E
Type: protein
Length: 371 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucanase
EC: 3.2.1.73
UniProt: P27051
Ligands: CA
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucanase (EC 3.2.1.73)	protein	185	0% helix, 50% strand	P27051
B	Beta-glucanase (EC 3.2.1.73)	protein	186	0% helix, 51% strand	P27051

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.36	0.75	19	empty

Compared structures

3D6E · Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
P27051 · AlphaFold monomer V2.0 prediction for beta-glucanase (P27051) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 P27051
Elsewhere: RCSB PDB 3D6E · PDBe 3D6E · UniProt P27051

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