Research workbench

Human butyrylcholinesterase in complex with propidium

Analyse Human butyrylcholinesterase in complex with propidium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ESJ
Type: protein
Length: 1,053 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cholinesterase
EC: 3.1.1.8
UniProt: P06276
Ligands: PRM, GLY, NAG, CL
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cholinesterase (EC 3.1.1.8)	protein	527	31% helix, 15% strand	P06276
B	Cholinesterase (EC 3.1.1.8)	protein	526	33% helix, 16% strand	P06276

Ligands and binding sites

PRM · 3,8-diamino-5[3-(diethylmethylammonio)propyl]-6-phenylphenanthridinium · ligand · 2 copies · chains A, B
GLY · Glycine · ligand · chains B
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains A, B
CL · Chloride ion · ion · 4 copies · chains B

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

Pockets

10 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	1072	0.80	0.81	86	NAG, PRM
2	553	0.78	0.84	45	PRM
3	386	0.61	0.77	44	CL
4	238	0.53	0.76	23	empty
5	171	0.47	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 774 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 glycan, 6 disulfide (N-glycosylation, disulfide).

Compared structures

6ESJ · Human butyrylcholinesterase in complex with propidium · the same entry in another collection · chain A against A, TM-score 1.00
P06276 · AlphaFold monomer V2.0 prediction for cholinesterase (P06276) · a predicted model of the same protein · chain B 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 P06276
Elsewhere: RCSB PDB 6ESJ · PDBe 6ESJ · UniProt P06276

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