1p0m

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spinqualitylabelsall models PDB ID 1p0m Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.38Å
Ligands:	, , , , and
Gene:	BCHE OR CHE1 (Homo sapiens)
Activity:	Cholinesterase, with EC number 3.1.1.8
Coordinates:	save as pdb, mmCIF, xml

Crystal structure of human butyryl cholinesterase in complex with a choline molecule

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave. Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding. As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase. The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected. An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.

Disease

Known diseases associated with this structure: Apnea, postanesthetic OMIM:[177400]

About this Structure

1P0M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products., Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F, J Biol Chem. 2003 Oct 17;278(42):41141-7. Epub 2003 Jul 17. PMID:12869558

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