4ZJS: PDB entry 4ZJS

Crystal structure of a chimeric acetylcholine binding protein from Aplysia Californica (Ac-AChBP) containing the main immunogenic region (MIR) from the human alpha 1 subunit of the muscle nicotinic acetylcholine receptor in complex with anatoxin-A. Determined by X-ray diffraction at 2.23 Å resolution. Released 13 May 2015.

Method: X-ray diffraction
Resolution: 2.23 Å
Organisms: Homo sapiens, Aplysia californica
Chains: 5
Atoms: 8,261
Mol. weight: 132.04 kDa
Ligands: 4P0
Released: 13 May 2015

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

Secondary structure: helices and β-sheets

4ZJS contains 25 α-helices and 75 β-strands across 5 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: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-11	9
α-helix	28	1
β-strand	29-44	16	1
β-strand	49-66	18	1
α-helix	69-72	4
β-strand	77-81	5	1
α-helix	82-84	3
β-strand	90-92	3	2
β-strand	95	1	1
α-helix	98-99	2
β-strand	100-101	2	1
β-strand	106-110	5	1
β-strand	112-117	6	1
β-strand	120-126	7	1
β-strand	138-146	9	2
β-strand	154-157	4	1
β-strand	162	1	2
β-strand	164	1	1
β-strand	174-186	13	2
β-strand	195-206	12	2

Chain B: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-12	10
α-helix	28	1
β-strand	29-44	16	3
β-strand	49-66	18	3
α-helix	69-72	4
β-strand	77-81	5	3
α-helix	82-84	3
β-strand	90-92	3	4
β-strand	95	1	3
α-helix	98-99	2
β-strand	100-101	2	3
β-strand	106-110	5	3
β-strand	112-117	6	3
β-strand	120-126	7	3
β-strand	138-146	9	4
β-strand	154-157	4	3
β-strand	162	1	4
β-strand	164	1	3
β-strand	174-186	13	4
β-strand	195-206	12	4

Chain C: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-12	10
α-helix	28	1
β-strand	29-44	16	5
β-strand	49-61	13	5
α-helix	69-72	4
β-strand	77-81	5	5
α-helix	82-84	3
β-strand	90-92	3	6
β-strand	95	1	5
α-helix	98-99	2
β-strand	100-101	2	5
β-strand	106-110	5	5
β-strand	114-117	4	5
β-strand	120-126	7	5
β-strand	138-146	9	6
β-strand	154-157	4	5
β-strand	162	1	6
β-strand	164	1	5
β-strand	174-186	13	6
β-strand	195-206	12	6

Chain D: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-12	10
β-strand	29-44	16	7
β-strand	49-66	18	7
α-helix	69-72	4
β-strand	77-81	5	7
α-helix	82-84	3
β-strand	90-92	3	8
β-strand	95	1	7
α-helix	98-99	2
β-strand	100-101	2	7
β-strand	106-110	5	7
β-strand	112-117	6	7
β-strand	120-126	7	7
β-strand	138-146	9	8
β-strand	154-157	4	7
β-strand	162	1	8
α-helix	163	1
β-strand	164	1	7
β-strand	174-188	15	8
β-strand	191-206	16	8

Chain E: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-12	10
α-helix	28	1
β-strand	29-44	16	9
β-strand	49-66	18	9
α-helix	69-72	4
β-strand	77-81	5	9
α-helix	82-84	3
β-strand	90-92	3	10
β-strand	95	1	9
α-helix	98-99	2
β-strand	100-101	2	9
β-strand	106-110	5	9
β-strand	112-117	6	9
β-strand	120-126	7	9
β-strand	138-146	9	10
β-strand	154-157	4	9
β-strand	162	1	10
β-strand	164	1	9
β-strand	175-188	14	10
β-strand	191-205	15	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholine receptor subunit alpha,Soluble acetylcholine receptor,Acetylcholine receptor subunit…	A, B, C, D, E	protein	230	Homo sapiens, Aplysia californica	P02708 (AlphaFold model), Q8WSF8 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>4ZJS_1 Acetylcholine receptor subunit alpha,Soluble acetylcholine receptor,Acetylcholine receptor subunit alpha,Soluble acetylcholine receptor (chains A, B, C, D, E)
DYKDDDDKLSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTLGFTLQDIVKADSSTNEVD
LVYYEQQRWVDYNLKWNPDDYGGVKKIHIPAADIWTPDITAYSSTRPVQVLSPQIAVVTH
DGSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYAS
SKYEILSATQTRQVQHYSCCPEPYIDVNLVVKFRERRAGNGFFRNLFDSR

Ligands and cofactors

ID	Name	Formula	Copies
4P0	1-[(1R,6R)-9-azabicyclo[4.2.1]non-2-en-2-yl]ethanone	C10 H15 N O	3

Primary citation

Main immunogenic region structure promotes binding of conformation-dependent myasthenia gravis autoantibodies, nicotinic acetylcholine receptor conformation maturation, and agonist sensitivity. Luo, J., Taylor, P., Losen, M. et al. J Neurosci (2009) 29:13898-13908. DOI 10.1523/JNEUROSCI.2833-09.2009 · PubMed

Other PDB entries of the same protein (UniProt P02708 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9DMS 1.92 Å, Human muscle nAChR with fab6-bound
9DMG 2.05 Å, Human muscle nAChR apo state
9DMH 2.06 Å, Human muscle nAChR ACh-bound state
9DMQ 2.06 Å, Human muscle nAChR with fab3-bound
9DMV 2.13 Å, Human muscle nAChR with fab9-bound
9DMT 2.18 Å, Human muscle nAChR with fab7-bound
9DMJ 2.19 Å, Human muscle nAChR with two fab1b-bound
9YER 2.19 Å, Human muscle nAChR SCCMS eT264P ACh bound
9YE8 2.22 Å, Human muscle nAChR SCCMS eL269F ACh bound
9DML 2.24 Å, Human muscle nAChR with fab2-bound
9YEI 2.36 Å, Human muscle nAChR SCCMS eL269F ACh, Reboxetine bound (lower 1)
9YET 2.36 Å, Human muscle nAChR SCCMS eT264P ACh, Reboxetine bound

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