Brand  (β version)

PDB ID: 5HFA

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Ligands
Code Name Style Show Link
DEP Diethyl phosphonate PoSSuM
EDO 1,2-ethanediol PoSSuM
FP1 N-hydroxy-1-(1-methylpyridin-2(1h)-ylidene)methanamine PoSSuM
NO3 Nitrate ion PoSSuM
Non-standard Residues
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Glycosylation
Code Name Emphasize
FUC Alpha-L-fucopyranose
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
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Structure summary

Code : 5HFA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of human acetylcholinesterase in complex with paraoxon and 2-PAM
Release Data : 2016-06-22
Compound :
mol_id molecule chains synonym
1 Acetylcholinesterase A,B AChE
ec: 3.1.1.7
fragment: catalytic domain, UNP residues 33 to 574
mutation: none
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Homo sapiens  (taxid:9606)
gene: ACHE
expression_system_cell_line: HEK293
Authors : Franklin, M.F., Rudolph, M.J., Ginter, C., Cassidy, M.S., Cheung, J.
Keywords : acetylcholinesterase, hydrolase
Exp. method : X-RAY DIFFRACTION ( 2.2010 Å )
Citation :

Structures of paraoxon-inhibited human acetylcholinesterase reveal perturbations of the acyl loop and the dimer interface.

Franklin, M.C.,Rudolph, M.J.,Ginter, C.  et al.
(2016)  Proteins  84 : 1246 - 1256

PubMed: 27191504
DOI: 10.1002/prot.25073

Reaction

Chain : A, B
UniProt : P22303 (ACES_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
acetylcholine + H2O = acetate + choline + H(+) 3.1.1.7 PubMed:1517212
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