4EY4: Acetylcholinesterase

Crystal Structure of Recombinant Human Acetylcholinesterase in the Apo state. Determined by X-ray diffraction at 2.16 Å resolution. Released 17 Oct 2012.

Method: X-ray diffraction
Resolution: 2.16 Å
Organism: Homo sapiens
Chains: 2
Atoms: 8,905
Mol. weight: 120.94 kDa
Ligands: NAG, PE8
Released: 17 Oct 2012

Explore 4EY4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4EY4 contains 73 α-helices and 51 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: 37 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	9-12	4	1
β-strand	15-18	4	1
β-strand	20-22	3	2
β-strand	29-32	4	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	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	136-142	7
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	204-213	10
α-helix	216-219	4
β-strand	224-228	5	2
β-strand	239-240	2	6
α-helix	241-254	14
α-helix	266-274	9
α-helix	278-284	7
α-helix	285-288	4
β-strand	302-303	2	6
α-helix	312-317	6
β-strand	325-331	7	2
β-strand	333	1	7
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	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	467-486	20
α-helix	490-491	2
α-helix	493	1
α-helix	501-502	2
β-strand	503	1	2
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	536-541	6

Chain B: 36 helices, 25 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	20-22	3	9
α-helix	23	1
β-strand	29-32	4	9
β-strand	33	1	10
β-strand	34-36	3	9
β-strand	38	1	11
α-helix	43-45	3
α-helix	49-51	3
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
α-helix	171-186	16
α-helix	187-190	4
β-strand	192-202	11	9
α-helix	204-213	10
α-helix	216-219	4
β-strand	224-228	5	9
β-strand	239	1	13
α-helix	241-254	14
α-helix	266-273	8
α-helix	278-282	5
α-helix	285-288	4
β-strand	302	1	13
α-helix	312-317	6
β-strand	325-331	7	9
β-strand	333	1	14
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	441-443	3
β-strand	446	1	14
α-helix	451-454	4
α-helix	457-459	3
α-helix	467-486	20
α-helix	498-499	2
α-helix	501-503	3
β-strand	509-513	5	9
α-helix	517-518	2
β-strand	519-522	4	9
α-helix	526-530	5
α-helix	531-535	5
α-helix	536-541	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholinesterase	A, B	protein	542	Homo sapiens	P22303 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4EY4_1 Acetylcholinesterase (chains A, B)
GREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVD
ATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGG
GFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQ
WVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGM
GEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVP
VVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLA
GVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQ
GARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWA
NFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLS
AT

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
PE8	3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol	C16 H34 O9	1

Water and common crystallization additives (NO3, EDO) are not listed.

Primary citation

Structures of human acetylcholinesterase in complex with pharmacologically important ligands. Cheung, J., Rudolph, M.J., Burshteyn, F. et al. J Med Chem (2012) 55:10282-10286. DOI 10.1021/jm300871x · PubMed

Other PDB entries of the same protein (UniProt P22303 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4M0E 2.0 Å, Structure of human acetylcholinesterase in complex with dihydrotanshinone I
6NTO 2.05 Å, Crystal Structure of Recombinant Human Acetylcholinesterase Inhibited by A-230
6O69 2.08 Å, Crystal Structure of Double Mutant L380R/F535K of Human Acetylcholinesterase
5HF5 2.15 Å, Crystal structure of human acetylcholinesterase in complex with paraoxon in the unaged…
6O5V 2.15 Å, Binary complex of native hAChE with oxime reactivator RS-170B
6WVO 2.19 Å, Crystal Structure of Recombinant Human Acetylcholinesterase In Complex with GD and HI-6
5HF9 2.2 Å, Crystal structure of human acetylcholinesterase in complex with paraoxon and HI6
5HFA 2.2 Å, Crystal structure of human acetylcholinesterase in complex with paraoxon and 2-PAM
8DT7 2.21 Å, X-ray structure of human acetylcholinesterase in complex with oxime MMB4 (hAChE-MMB4)
6CQZ 2.22 Å, Crystal Structure of Recombinant Human Acetylcholinesterase Inhibited by VX
6NTL 2.25 Å, Crystal Structure of Recombinant Human Acetylcholinesterase Inhibited by A-234
6U37 2.25 Å, Structure of VX-phosphonylated hAChE in complex with oxime reactivator RS194B

Browse structure collections

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