MolNFT v1 · #73566 · protein

Crystal structure of the endo-beta-1,3-1,4 glucanase from bacillus subtilis (strain 168)

3O5S · Beta-glucanase: “Crystal structure of the endo-beta-1,3-1,4 glucanase from bacillus subtilis (strain 168)”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.52). MolNFT v1 #73566 on GenesisL1: 3D structure, binding…

PDB: 3O5S
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucanase
EC: 3.2.1.73
UniProt: P04957
Ligands: CA
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucanase (EC 3.2.1.73)	protein	213	6% helix, 52% strand	P04957

Ligands and binding sites

CA · Calcium ion · metal · chains A
B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.52	0.78	25	B3P

Compared structures

3O5S · Crystal Structure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168) · the same entry in another collection · chain A against A, TM-score 1.00
P04957 · AlphaFold monomer V2.0 prediction for beta-glucanase (P04957) · 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 P04957
Elsewhere: RCSB PDB 3O5S · PDBe 3O5S · UniProt P04957

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