7AIS: Torpedo Californica acetylcholinesterase

Crystal structure of Torpedo Californica acetylcholinesterase in complex with 6-[(3-Chloro-6,7,10,11-tetrahydro-9-methyl-7,11-methanocycloocta[b]quinolin-12-yl)amino]-N-(4-hydroxy-3-methoxybenzyl)hexanamide. Determined by X-ray diffraction at 1.75 Å resolution. Released 6 Oct 2021.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Tetronarce californica
Chains
2
Atoms
9,823
Mol. weight
134.5 kDa
Ligands
NAG, 8UH
Released
6 Oct 2021

Explore 7AIS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7AIS contains 76 α-helices and 56 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 38 helices, 28 β-strands

ElementResiduesLengthSheet
β-strand7-1041
β-strand13-1641
β-strand18-2252
β-strand25-3062
β-strand3113
β-strand32-3432
β-strand3614
α-helix41-433
α-helix47-482
β-strand5014
α-helix51-533
β-strand57-5931
β-strand6113
α-helix651
β-strand6615
α-helix67-682
α-helix79-824
β-strand9015
β-strand96-10162
α-helix105-1062
β-strand109-11572
α-helix128-1303
α-helix133-1397
β-strand142-14542
α-helix151-1555
β-strand15716
β-strand16516
α-helix168-18316
α-helix184-1874
β-strand189-199112
α-helix201-21111
α-helix216-2183
β-strand221-22552
β-strand236-23727
α-helix238-25114
α-helix259-26810
α-helix271-2766
α-helix278-2814
β-strand295-29627
α-helix305-3117
β-strand319-32462
β-strand32618
α-helix329-3357
α-helix349-35911
α-helix365-37410
α-helix384-39613
α-helix397-4015
α-helix402-41413
β-strand418-42362
α-helix425-4273
α-helix434-4363
β-strand43918
α-helix444-4474
α-helix450-4523
α-helix454-4563
α-helix460-47920
α-helix4841
α-helix490-4912
α-helix493-4942
β-strand49512
β-strand501-50552
α-helix509-5102
β-strand512-51432
α-helix518-5225
α-helix523-5275
α-helix528-5347
Chain B: 38 helices, 28 β-strands
ElementResiduesLengthSheet
β-strand7-1049
β-strand13-1649
β-strand18-22510
β-strand25-30610
β-strand31111
β-strand32-34310
β-strand36112
α-helix41-433
α-helix47-482
β-strand50112
α-helix51-533
β-strand57-5939
β-strand61111
α-helix651
β-strand66113
α-helix67-682
α-helix79-824
β-strand90113
β-strand96-101610
α-helix105-1062
β-strand109-115710
α-helix128-1303
α-helix133-1397
β-strand142-145410
α-helix151-1555
β-strand157114
β-strand165114
α-helix168-18316
α-helix184-1874
β-strand189-1991110
α-helix201-21111
α-helix213-2164
β-strand221-225510
β-strand236-237215
α-helix238-25114
α-helix259-26810
α-helix271-2777
α-helix278-2814
β-strand295-296215
α-helix305-3117
β-strand319-324610
β-strand326116
α-helix329-3357
α-helix349-35911
α-helix365-37511
α-helix384-39613
α-helix397-4015
α-helix402-41211
β-strand418-423610
α-helix425-4273
α-helix434-4363
β-strand439116
α-helix444-4474
α-helix450-4523
α-helix454-4563
α-helix460-47920
α-helix4841
α-helix490-4912
α-helix493-4942
β-strand495110
β-strand501-505510
α-helix5101
β-strand512-514310
α-helix519-5224
α-helix523-5275
α-helix528-5347

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AcetylcholinesteraseA, Bprotein586Tetronarce californicaP04058 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7AIS_1 Acetylcholinesterase (chains A, B)
MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPP
VGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNI
WVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALH
GSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLF
RRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEW
NVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGF
SKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHN
VICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYT
AEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQ
MCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O65
8UH6-[(3-Chloro-6,7,10,11-tetrahydro-9-methyl-7,11-methanocycloocta[b]quinolin-12-…C31 H36 Cl N3 O32

Water and common crystallization additives (CL, PEG) are not listed.

Primary citation

Discovery of a Potent Dual Inhibitor of Acetylcholinesterase and Butyrylcholinesterase with Antioxidant Activity that Alleviates Alzheimer-like Pathology in Old APP/PS1 Mice. Viayna, E., Coquelle, N., Cieslikiewicz-Bouet, M. et al. J Med Chem (2021) 64:812-839. DOI 10.1021/acs.jmedchem.0c01775 · PubMed

Other PDB entries of the same protein (UniProt P04058 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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