6G1W: Torpedo Californica acetylcholinesterase

Crystal structure of Torpedo Californica acetylcholinesterase in complex with 2-{1-[2-(6-Chloro-1,2,3,4-tetrahydroacridin-9-ylamino)ethyl]-1H-1,2,3-triazol-4-yl}-N-[4-(hydroxy)-3-methoxybenzyl]acetamide. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Apr 2018.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Tetronarce californica
Chains: 2
Atoms: 9,640
Mol. weight: 130.07 kDa
Ligands: E0Z, NAG
Released: 4 Apr 2018

Explore 6G1W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G1W contains 72 α-helices and 55 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: 35 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	1
β-strand	13-16	4	1
β-strand	18-22	5	2
β-strand	25-30	6	2
β-strand	31	1	3
β-strand	32-34	3	2
β-strand	36	1	4
α-helix	41-43	3
α-helix	47-48	2
β-strand	50	1	4
α-helix	51-53	3
β-strand	57-59	3	1
β-strand	61	1	3
α-helix	65	1
β-strand	66	1	5
α-helix	67-68	2
α-helix	79-82	4
β-strand	90	1	5
β-strand	96-101	6	2
α-helix	105-106	2
β-strand	109-115	7	2
α-helix	128-130	3
α-helix	133-139	7
β-strand	142-145	4	2
α-helix	152-155	4
β-strand	157	1	6
β-strand	165	1	6
α-helix	168-183	16
α-helix	184-187	4
β-strand	189-199	11	2
α-helix	201-211	11
α-helix	216-218	3
β-strand	221-225	5	2
β-strand	236-237	2	7
α-helix	238-251	14
α-helix	259-268	10
α-helix	271-275	5
α-helix	278-281	4
β-strand	295-296	2	7
α-helix	305-311	7
β-strand	319-324	6	2
β-strand	326	1	8
α-helix	329-335	7
α-helix	349-359	11
α-helix	365-375	11
α-helix	384-396	13
α-helix	397-401	5
α-helix	402-414	13
β-strand	418-423	6	2
α-helix	434-436	3
β-strand	439	1	8
α-helix	444-447	4
α-helix	450-452	3
α-helix	454-456	3
α-helix	460-479	20
α-helix	493-495	3
β-strand	501-505	5	2
α-helix	509-510	2
β-strand	512-514	3	2
α-helix	518-522	5
α-helix	523-527	5
α-helix	528-534	7

Chain B: 37 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	9
β-strand	13-16	4	9
β-strand	18-22	5	10
β-strand	25-30	6	10
β-strand	31	1	11
β-strand	32-34	3	10
β-strand	36	1	12
α-helix	41-43	3
α-helix	47-48	2
β-strand	50	1	12
α-helix	51-53	3
β-strand	57-59	3	9
β-strand	61	1	11
α-helix	65	1
β-strand	66	1	13
α-helix	67-68	2
α-helix	79-82	4
β-strand	90	1	13
β-strand	96-101	6	10
α-helix	105-106	2
β-strand	109-115	7	10
α-helix	128-130	3
α-helix	133-139	7
β-strand	142-145	4	10
α-helix	151-155	5
β-strand	159	1	14
β-strand	161	1	14
α-helix	168-183	16
α-helix	184-187	4
β-strand	189-199	11	10
α-helix	201-211	11
α-helix	213-216	4
β-strand	221-225	5	10
β-strand	236-237	2	15
α-helix	238-250	13
α-helix	259-268	10
α-helix	271-277	7
α-helix	278-281	4
β-strand	295-296	2	15
α-helix	305-311	7
β-strand	319-324	6	10
β-strand	326	1	16
α-helix	329-335	7
α-helix	349-359	11
α-helix	365-375	11
α-helix	384-396	13
α-helix	397-401	5
α-helix	402-412	11
β-strand	418-423	6	10
α-helix	425-427	3
α-helix	434-436	3
β-strand	439	1	16
α-helix	444-447	4
α-helix	450-452	3
α-helix	454-456	3
α-helix	460-479	20
α-helix	490-491	2
α-helix	493-494	2
β-strand	495	1	10
β-strand	501-505	5	10
α-helix	510	1
β-strand	512-514	3	10
α-helix	518-522	5
α-helix	523-527	5
α-helix	528-532	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholinesterase	A, B	protein	565	Tetronarce californica	P04058 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6G1W_1 Acetylcholinesterase (chains A, B)
DDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNA
STYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGF
YSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWV
HDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAE
GRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEF
FPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSV
PHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYL
YFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTG
NPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGE
LSSSGTSSSKGIIFYVLFSILYLIF

Ligands and cofactors

ID	Name	Formula	Copies
E0Z	2-[1-[2-[(3-chloranylacridin-9-yl)amino]ethyl]-1,2,3-triazol-4-yl]-~{N}-[(3-met…	C27 H25 Cl N6 O3	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	6

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

Primary citation

Increasing Polarity in Tacrine and Huprine Derivatives: Potent Anticholinesterase Agents for the Treatment of Myasthenia Gravis. Galdeano, C., Coquelle, N., Cieslikiewicz-Bouet, M. et al. Molecules (2018) 23. DOI 10.3390/molecules23030634 · PubMed

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

7AIS 1.75 Å, Crystal structure of Torpedo Californica acetylcholinesterase in complex with…
6G1U 1.79 Å, Crystal structure of Torpedo Californica acetylcholinesterase in complex with…
1EA5 1.8 Å, NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA at 1.8A resolution
6G1V 1.82 Å, Crystal structure of Torpedo Californica acetylcholinesterase in complex with…
7B38 1.85 Å, Torpedo californica acetylcholinesterase complexed with Mg+2
6H14 1.86 Å, Crystal structure of TcACHE complexed to 1-(6-oxo-1,2,3,4,6,10b-hexahydropyrido[2,1-a]iso…
7AIX 1.86 Å, Crystal structure of Torpedo Californica acetylcholinesterase in complex with…
7AIW 1.9 Å, Crystal structure of Torpedo Californica acetylcholinesterase in complex with…
2C5G 1.95 Å, Torpedo californica acetylcholinesterase in complex with 20mM thiocholine
2WFZ 1.95 Å, Non-aged conjugate of torpedo californica acetylcholinesterase with soman
2WG2 1.95 Å, Non-aged conjugate of torpedo californica acetylcholinesterase with soman (alternative…
7AIU 2.0 Å, Crystal structure of Torpedo Californica acetylcholinesterase in complex with…

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