Research workbench

GH115 alpha-1,2-glucuronidase in complex with xylopentaose

Analyse GH115 alpha-1,2-glucuronidase in complex with xylopentaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PUG
Type: protein
Length: 829 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylan alpha-1,2-glucuronidase
EC: 3.2.1.131
Ligands: XYP, CA, CL
Pockets: 7 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylan alpha-1,2-glucuronidase (EC 3.2.1.131)	protein	829	36% helix, 19% strand	—

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 5 copies · chains A
CA · Calcium ion · metal · 3 copies · chains A
CL · Chloride ion · ion · 13 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	479	0.69	0.80	50	empty
2	316	0.58	0.77	25	empty
3	66	0.54	0.87	16	empty
4	123	0.46	0.78	22	XYP
5	86	0.46	0.81	20	empty

Compared structures

7PUG · GH115 alpha-1,2-glucuronidase in complex with xylopentaose · 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
Elsewhere: RCSB PDB 7PUG · PDBe 7PUG

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