6U37: VX-phosphonylated hAChE

Structure of VX-phosphonylated hAChE in complex with oxime reactivator RS194B. Determined by X-ray diffraction at 2.25 Å resolution. Released 12 Feb 2020.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Homo sapiens
Chains: 2
Atoms: 8,830
Mol. weight: 121.81 kDa
Ligands: VX, PQV
Released: 12 Feb 2020

Explore 6U37 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6U37 contains 73 α-helices and 44 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, 22 β-strands

Element	Residues	Length	Sheet
α-helix	5-8	4
β-strand	9-11	3	1
β-strand	16-18	3	1
β-strand	20-22	3	2
β-strand	29-36	8	2
β-strand	38	1	3
α-helix	43-45	3
β-strand	52	1	3
α-helix	53-55	3
β-strand	59-61	3	1
β-strand	63	1	2
α-helix	67	1
β-strand	68	1	4
α-helix	69	1
α-helix	81-84	4
β-strand	92	1	4
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	155-158	4
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	1	5
α-helix	241-254	14
α-helix	259	1
α-helix	266-274	9
α-helix	278-282	5
α-helix	286-288	3
β-strand	302	1	5
α-helix	312-317	6
β-strand	325-331	7	2
α-helix	337-341	5
α-helix	356-366	11
α-helix	372-382	11
α-helix	391-403	13
α-helix	404-408	5
α-helix	409-419	11
β-strand	424-430	7	2
α-helix	432-434	3
α-helix	441-443	3
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
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, 22 β-strands

Element	Residues	Length	Sheet
α-helix	5-8	4
β-strand	9-11	3	6
β-strand	16-18	3	6
β-strand	20-22	3	7
β-strand	29-36	8	7
β-strand	38	1	8
α-helix	43-45	3
α-helix	49-51	3
β-strand	52	1	8
α-helix	53-55	3
β-strand	59-61	3	6
β-strand	63	1	7
α-helix	67	1
β-strand	68	1	9
α-helix	69	1
α-helix	81-84	4
β-strand	92	1	9
β-strand	98-104	7	7
α-helix	107-108	2
β-strand	112-118	7	7
α-helix	131-133	3
α-helix	136-142	7
β-strand	145-149	5	7
α-helix	155-158	4
α-helix	171-186	16
α-helix	187-190	4
β-strand	192-202	11	7
α-helix	204-213	10
α-helix	216-219	4
β-strand	224-228	5	7
β-strand	239	1	10
α-helix	241-254	14
α-helix	266-275	10
α-helix	278-282	5
α-helix	286-288	3
β-strand	302	1	10
α-helix	312-317	6
β-strand	325-331	7	7
α-helix	337-341	5
α-helix	356-366	11
α-helix	372-381	10
α-helix	391-403	13
α-helix	404-408	5
α-helix	409-419	11
β-strand	424-430	7	7
α-helix	441-443	3
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	7
β-strand	509-513	5	7
α-helix	517-518	2
β-strand	520-522	3	7
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	550	Homo sapiens	P22303 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6U37_1 Acetylcholinesterase (chains A, B)
GPLEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWS
GVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVW
IYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQR
LALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWA
TVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRF
SFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRA
EFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGR
LAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLM
RYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLP
KLLSATDTLD

Ligands and cofactors

ID	Name	Formula	Copies
VX	O-ethylmethylphosphonic acid ester group	C3 H9 O3 P	2
PQV	(2E)-N-[2-(azepan-1-yl)ethyl]-2-(hydroxyimino)acetamide	C10 H19 N3 O2	2

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

Primary citation

Rational design, synthesis, and evaluation of uncharged, "smart" bis-oxime antidotes of organophosphate-inhibited human acetylcholinesterase. Gorecki, L., Gerlits, O., Kong, X. et al. J Biol Chem (2020) 295:4079-4092. DOI 10.1074/jbc.RA119.012400 · 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
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

Browse structure collections

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