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Crystal structure of laminaripentaose-producing beta-1,3- glucanase

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

PDB: 3GD0
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Laminaripentaose-producing beta-1,3-guluase (lphase)
EC: 3.2.1.39
UniProt: Q9Z4I2
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Laminaripentaose-producing beta-1,3-guluase (lphase) (EC 3.2.1.39)	protein	362	18% helix, 32% strand	Q9Z4I2

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	85	0.33	0.74	16	empty

Compared structures

3GD0 · Crystal structure of laminaripentaose-producing beta-1,3-glucanase · 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
Every structure of UniProt Q9Z4I2
Elsewhere: RCSB PDB 3GD0 · PDBe 3GD0 · UniProt Q9Z4I2

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