MolNFT v1 · #147888 · protein

Human butyrylcholinesterase in complex with ethopropazine

6EQP: “Human butyrylcholinesterase in complex with ethopropazine”. X-ray diffraction, 7 ligands (BUW, NAG, FUL). MolNFT v1 #147888 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6EQP
Type: protein
Length: 526 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P06276
Ligands: BUW, NAG, FUL, FUC, ZN, CL, SO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	526	—	P06276

Ligands and binding sites

BUW · R-ethopropazine · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
FUL · beta-L-fucopyranose · sugar · 2 copies · chains A
FUC · alpha-L-fucopyranose · sugar · chains A
ZN · Zinc ion · metal
CL · Chloride ion · ion · 7 copies · chains A
SO4 · Sulfate ion · ion · chains A

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

Compared structures

6EQP · Human butyrylcholinesterase in complex with ethopropazine · 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 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 P06276
Elsewhere: RCSB PDB 6EQP · PDBe 6EQP · UniProt P06276

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