Research workbench

A new GH20 apo enzyme from bacteroides thetaiotaomicron

Analyse A new GH20 apo enzyme from bacteroides thetaiotaomicron in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DUP
Type: protein
Length: 524 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-N-acetylhexosaminidase
EC: 3.2.1.52
UniProt: A0A0P0FIE8
Ligands: CL
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-N-acetylhexosaminidase (EC 3.2.1.52)	protein	524	39% helix, 20% strand	A0A0P0FIE8

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	202	0.57	0.80	29	GOL
2	163	0.56	0.81	25	empty
3	55	0.26	0.73	13	empty

Compared structures

7DUP · Apo structure of wild type Bt4394, a GH20 family sulfoglycosidase · 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 A0A0P0FIE8
Elsewhere: RCSB PDB 7DUP · PDBe 7DUP · UniProt A0A0P0FIE8

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