MolNFT v1 · #61278 · protein

The 1.5 a crystal structure of endo-1,3-beta-glucanase from streptomyces sioyaensis

3DGT: “The 1.5 a crystal structure of endo-1,3-beta-glucanase from streptomyces sioyaensis”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.65). MolNFT v1 #61278 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3DGT
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,3-beta-glucanase
EC: 3.2.1.39
UniProt: Q9L816
Ligands: MG
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,3-beta-glucanase (EC 3.2.1.39)	protein	278	9% helix, 39% strand	Q9L816

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

2 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	259	0.65	0.82	28	empty
2	68	0.34	0.76	20	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3DGT · The 1.5 A crystal structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis · 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 Q9L816
Elsewhere: RCSB PDB 3DGT · PDBe 3DGT · UniProt Q9L816

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