MolNFT v1 · #7930 · protein

Cation binding to a bacillus (1,3-1,4)-beta-glucanase. geometry, affinity and effect on protein stability

1GLH · 1,3-1,4-beta-glucanase: “Cation binding to a bacillus (1,3-1,4)-beta-glucanase. geometry, affinity and effect on protein stability”. X-ray diffraction, 1 ligand (NA), 1 pocket (best druggability 0.48). MolNFT v1 #7930 on GenesisL1…

PDB: 1GLH
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1,3-1,4-beta-glucanase
EC: 3.2.1.73
UniProt: P23904
Ligands: NA
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	1,3-1,4-beta-glucanase (EC 3.2.1.73)	protein	214	6% helix, 53% strand	P23904

Ligands and binding sites

NA · Sodium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.48	0.77	22	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1GLH · Cation binding to a bacillus (1,3-1,4)-beta-glucanase. geometry, affinity and effect on… · the same entry in another collection · chain A against A, TM-score 1.00
P23904 · AlphaFold monomer V2.0 prediction for beta-glucanase (P23904) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P23904
Elsewhere: RCSB PDB 1GLH · PDBe 1GLH · UniProt P23904

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