Research workbench

Crystal structure of the GH26 domain from PBGH26-GH5A endo-beta- MANNANASE/ENDO-beta-glucanase from prevotella bryantii

Analyse Crystal structure of the GH26 domain from PBGH26-GH5A endo-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6D2X
Type: protein
Length: 336 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aryl-phospho-beta-D-glucosidase bglc, GH1 family
UniProt: D8DY19
Ligands: SO4
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aryl-phospho-beta-D-glucosidase bglc, GH1 family	protein	336	35% helix, 17% strand	D8DY19

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A
PE3 · 3,6,9,12,15,18,21,24,27,30,33,36,39-tridecaoxahentetracontane-1,41-diol · additive · 5 copies · chains A
GOL · Glycerol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.37	0.74	14	empty
2	56	0.24	0.72	13	empty

Compared structures

6D2X · Crystal structure of the GH26 domain from PbGH26-GH5A… · 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 D8DY19
Elsewhere: RCSB PDB 6D2X · PDBe 6D2X · UniProt D8DY19

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