Research workbench

Bacteroides ovatus xyloglucan pul GH31

Analyse Bacteroides ovatus xyloglucan pul GH31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JOU
Type: protein
Length: 945 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-xylosidase BOGH31A
EC: 3.2.1.177
UniProt: A7LXT0
Ligands: NI
Pockets: 11 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-xylosidase BOGH31A (EC 3.2.1.177)	protein	945	22% helix, 33% strand	A7LXT0

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
EDO · 1,2-ethanediol · additive · 9 copies · chains A

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	265	0.75	0.89	32	EDO
2	121	0.58	0.85	29	empty
3	151	0.53	0.80	29	EDO
4	127	0.50	0.80	26	empty
5	197	0.49	0.76	28	empty

Compared structures

5JOU · Bacteroides ovatus Xyloglucan PUL GH31 · the same entry in another collection · chain A against A, TM-score 1.00
A7LXT0 · AlphaFold monomer V2.0 prediction for alpha-xylosidase BOGH31A (A7LXT0) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 A7LXT0
Elsewhere: RCSB PDB 5JOU · PDBe 5JOU · UniProt A7LXT0

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