5FOQ: Acetylcholinesterase

Acetylcholinesterase in complex with C7653. Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Mar 2016.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: MUS MUSCULUS
Chains: 2
Atoms: 8,777
Mol. weight: 122.7 kDa
Ligands: P15, PG0, GC8, NAG
Released: 2 Mar 2016

Explore 5FOQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FOQ contains 73 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, 25 β-strands

Element	Residues	Length	Sheet
β-strand	9-12	4	1
β-strand	15-18	4	1
β-strand	20-24	5	2
β-strand	27-32	6	2
β-strand	33	1	3
β-strand	34-36	3	2
β-strand	38	1	4
α-helix	43-45	3
α-helix	49-50	2
β-strand	52	1	4
α-helix	53-55	3
β-strand	59-61	3	1
β-strand	63	1	3
α-helix	67	1
β-strand	68-69	2	5
α-helix	72-74	3
α-helix	81-84	4
β-strand	92-93	2	5
β-strand	98-104	7	2
α-helix	107-108	2
β-strand	112-118	7	2
α-helix	131-133	3
α-helix	136-137	2
α-helix	138-142	5
β-strand	145-149	5	2
α-helix	154-158	5
α-helix	171-186	16
α-helix	187-190	4
β-strand	192-202	11	2
α-helix	204-214	11
α-helix	216-219	4
β-strand	224-228	5	2
β-strand	239	1	6
α-helix	241-254	14
α-helix	266-274	9
α-helix	278-283	6
α-helix	285-288	4
β-strand	302	1	6
α-helix	312-318	7
β-strand	325-331	7	2
β-strand	333	1	7
α-helix	336-341	6
α-helix	356-366	11
α-helix	372-382	11
α-helix	391-403	13
α-helix	404-408	5
α-helix	409-420	12
β-strand	424-430	7	2
α-helix	432-434	3
α-helix	441-443	3
β-strand	446	1	7
α-helix	451-454	4
α-helix	457-459	3
α-helix	461-463	3
α-helix	467-486	20
α-helix	498-499	2
α-helix	501-503	3
β-strand	509-513	5	2
α-helix	517-518	2
β-strand	519-522	4	2
α-helix	526-530	5
α-helix	531-535	5
α-helix	536-540	5

Chain B: 35 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	9-12	4	8
β-strand	15-18	4	8
β-strand	20-24	5	9
β-strand	27-32	6	9
β-strand	33	1	10
β-strand	34-36	3	9
β-strand	38	1	11
α-helix	43-45	3
α-helix	49-50	2
β-strand	52	1	11
α-helix	53-55	3
β-strand	59-61	3	8
β-strand	63	1	10
α-helix	67	1
β-strand	68-69	2	12
α-helix	81-84	4
β-strand	92-93	2	12
β-strand	98-104	7	9
α-helix	107-108	2
β-strand	112-118	7	9
α-helix	131-133	3
α-helix	136-142	7
β-strand	145-149	5	9
α-helix	154-158	5
β-strand	160	1	13
β-strand	168	1	13
α-helix	171-186	16
α-helix	187-190	4
β-strand	192-202	11	9
α-helix	204-213	10
α-helix	216-221	6
β-strand	224-228	5	9
β-strand	239-240	2	14
α-helix	241-254	14
α-helix	266-274	9
α-helix	278-282	5
α-helix	285-288	4
β-strand	302-303	2	14
α-helix	312-318	7
β-strand	325-331	7	9
β-strand	333	1	15
α-helix	336-339	4
α-helix	356-366	11
α-helix	372-382	11
α-helix	391-403	13
α-helix	404-408	5
α-helix	409-420	12
β-strand	424-430	7	9
α-helix	432-434	3
α-helix	441-443	3
β-strand	446	1	15
α-helix	451-454	4
α-helix	457-459	3
α-helix	461-463	3
α-helix	467-486	20
α-helix	501-502	2
β-strand	503	1	9
β-strand	509-513	5	9
β-strand	519-522	4	9
α-helix	526-530	5
α-helix	531-535	5
α-helix	536-542	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholinesterase	A, B	protein	548	MUS MUSCULUS	P21836 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5FOQ_1 ACETYLCHOLINESTERASE (chains A, B)
EGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVL
DATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYG
GGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLAL
QWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVS
AGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFV
PVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFL
AGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAA
QGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYW
TNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLL
SATATEAP

Ligands and cofactors

ID	Name	Formula	Copies
P15	2,5,8,11,14,17-hexaoxanonadecan-19-ol	C13 H28 O7	1
PG0	2-(2-methoxyethoxy)ethanol	C5 H12 O3	4
GC8	2-(2,4-dichlorophenoxy)-N-[4-(1-piperidinylmethyl)phenyl]acetamide	C20 H22 Cl2 N2 O2	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

Primary citation

The Nature of Activated Non-Classical Hydrogen Bonds: A Case Study on Acetylcholinesterase-Ligand Complexes. Berg, L., Mishra, B.K., Andersson, C.D. et al. Chemistry (2016) 22:2672. DOI 10.1002/CHEM.201503973 · PubMed

Other PDB entries of the same protein (UniProt P21836 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5DTI 2.0 Å, Crystal structure of mouse acetylcholinesterase
2HA2 2.05 Å, Crystal structure of mouse acetylcholinesterase complexed with succinylcholine
4B82 2.1 Å, Mus musculus Acetylcholinesterase in complex with N-(2-Diethylamino-…
4B85 2.1 Å, Mus musculus Acetylcholinesterase in complex with 4-Chloranyl-N-(2-…
5EIE 2.1 Å, mAChE-TZ2 complex
8ORC 2.1 Å, Mus Musculus Acetylcholinesterase in complex with AL237
2HA5 2.15 Å, Crystal structure of mutant S203A of acetylcholinesterase complexed with acetylthiocholine
2WHQ 2.15 Å, Crystal structure of acetylcholinesterase, phosphonylated by sarin (aged) in complex…
1N5M 2.2 Å, Crystal structure of the mouse acetylcholinesterase-gallamine complex
2GYU 2.2 Å, Crystal structure of Mus musculus Acetylcholinesterase in complex with HI-6
2HA0 2.2 Å, Crystal structure of mouse acetylcholinesterase complexed with 4-ketoamyltrimethylammonium
2WHP 2.2 Å, Crystal structure of acetylcholinesterase, phosphonylated by sarin and in complex with…

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