5HF5: Human acetylcholinesterase

Crystal structure of human acetylcholinesterase in complex with paraoxon in the unaged state (predominant acyl loop conformation). Determined by X-ray diffraction at 2.15 Å resolution. Released 27 Jul 2016.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 9,256
Mol. weight: 121.21 kDa
Ligands: DEP, PE8, NAG
Released: 27 Jul 2016

Explore 5HF5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5HF5 contains 73 α-helices and 52 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: 36 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	49-51	3
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	1	5
α-helix	69	1
α-helix	81-84	4
β-strand	92	1	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	266-275	10
α-helix	278-285	8
α-helix	286-288	3
β-strand	302-303	2	6
α-helix	312-318	7
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	498-499	2
α-helix	501-502	2
β-strand	503	1	2
β-strand	509-513	5	2
β-strand	519-522	4	2
α-helix	526-530	5
α-helix	531-535	5
α-helix	536-541	6

Chain B: 37 helices, 26 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	1	12
α-helix	69	1
α-helix	81-84	4
β-strand	92	1	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	239-240	2	13
α-helix	241-254	14
α-helix	266-273	8
α-helix	278-284	7
α-helix	285-288	4
β-strand	302-303	2	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	501-502	2
β-strand	503	1	9
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

>5HF5_1 Acetylcholinesterase (chains A, B)
GREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVD
ATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGG
GFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQ
WVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGM
GEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVP
VVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLA
GVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQ
GARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWA
NFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLS
AT

Ligands and cofactors

ID	Name	Formula	Copies
DEP	Diethyl phosphonate	C4 H11 O3 P	2
PE8	3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol	C16 H34 O9	1
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

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

Primary citation

Structures of paraoxon-inhibited human acetylcholinesterase reveal perturbations of the acyl loop and the dimer interface. Franklin, M.C., Rudolph, M.J., Ginter, C. et al. Proteins (2016) 84:1246-1256. DOI 10.1002/prot.25073 · 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
6O5V 2.15 Å, Binary complex of native hAChE with oxime reactivator RS-170B
4EY4 2.16 Å, Crystal Structure of Recombinant Human Acetylcholinesterase in the Apo state
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

About this viewer

MolViewer shows 5HF5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.