7AIW: Torpedo Californica acetylcholinesterase

Crystal structure of Torpedo Californica acetylcholinesterase in complex with (E)-10-[(3-Chloro-6,7,10,11-tetrahydro-9-methyl-7,11-methanocycloocta[b]quinolin-12-yl)amino]-N-(4-hydroxy-3-methoxybenzyl)-6-decenamide. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 Oct 2021.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Tetronarce californica
Chains
2
Atoms
9,783
Mol. weight
134.93 kDa
Ligands
8U5, NAG
Released
6 Oct 2021

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

Secondary structure: helices and β-sheets

7AIW contains 75 α-helices and 53 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, 26 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-helix70-723
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
α-helix168-18316
α-helix184-1874
β-strand189-199112
α-helix201-21111
α-helix213-2164
β-strand221-22552
β-strand236-23726
α-helix238-25013
α-helix259-26810
α-helix271-2777
α-helix278-2814
β-strand295-29626
α-helix305-3117
β-strand319-32462
β-strand32617
α-helix329-3357
α-helix349-35911
α-helix365-37511
α-helix384-39613
α-helix397-4015
α-helix402-41211
β-strand418-42362
α-helix425-4273
α-helix434-4363
β-strand43917
α-helix444-4474
α-helix450-4523
α-helix454-4563
α-helix460-47920
α-helix490-4912
α-helix493-4942
β-strand49512
β-strand501-50552
α-helix5101
β-strand512-51432
α-helix518-5225
α-helix523-5275
α-helix528-5336
Chain B: 37 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand7-1048
β-strand13-1648
β-strand18-2259
β-strand25-3069
β-strand31110
β-strand32-3439
β-strand36111
α-helix41-433
α-helix47-482
β-strand50111
α-helix51-533
β-strand57-5938
β-strand61110
α-helix651
β-strand66112
α-helix67-682
α-helix79-824
β-strand90112
β-strand96-10169
α-helix105-1062
β-strand109-11579
α-helix128-1303
α-helix133-1397
β-strand142-14549
α-helix152-1554
β-strand157113
β-strand165113
α-helix168-18316
α-helix184-1874
β-strand189-199119
α-helix201-21111
α-helix213-2186
β-strand221-22559
β-strand236-237214
α-helix238-25114
α-helix259-26810
α-helix271-2766
α-helix278-2814
β-strand295-296214
α-helix305-3117
β-strand319-32469
β-strand326115
α-helix329-3357
α-helix349-35911
α-helix365-37410
α-helix384-39613
α-helix397-4015
α-helix402-41413
β-strand418-42369
α-helix425-4273
α-helix434-4363
β-strand439115
α-helix444-4474
α-helix450-4523
α-helix454-4563
α-helix460-47920
α-helix490-4912
α-helix493-4953
β-strand501-50559
α-helix509-5102
β-strand512-51439
α-helix518-5225
α-helix523-5275
α-helix528-5347

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AcetylcholinesteraseA, Bprotein586Tetronarce californicaP04058 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7AIW_1 Acetylcholinesterase (chains A, B)
MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPP
VGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNI
WVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALH
GSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLF
RRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEW
NVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGF
SKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHN
VICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYT
AEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQ
MCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF

Ligands and cofactors

IDNameFormulaCopies
8U5E)-10-[(3-Chloro-6,7,10,11-tetrahydro-9-methyl-7,11-methanocycloocta[b]quinolin…C35 H46 Cl N3 O32
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O66

Water and common crystallization additives (MES, PEG, CL) 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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