5HBT: Acetylcholine receptor subunit alpha 1

Complex structure of Fab35 and human nAChR alpha1. Determined by X-ray diffraction at 2.61 Å resolution. Released 3 May 2017.

Method: X-ray diffraction
Resolution: 2.61 Å
Organisms: Homo sapiens, Rattus norvegicus, Bungarus multicinctus
Chains: 4
Atoms: 5,784
Mol. weight: 81.49 kDa
Released: 3 May 2017

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

Secondary structure: helices and β-sheets

5HBT contains 29 α-helices and 66 β-strands across 4 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: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	14
β-strand	5	1	15
β-strand	12	1	15
α-helix	14	1
β-strand	15	1	14
α-helix	16-17	2
β-strand	22-28	7	3
α-helix	33-36	4
β-strand	39-45	7	3
α-helix	48-50	3
β-strand	56-60	5	3

Chain B: 8 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	1-12	12
β-strand	29-44	16	1
β-strand	49-61	13	1
α-helix	63-65	3
α-helix	69-72	4
β-strand	77-81	5	1
α-helix	82-84	3
β-strand	90-93	4	2
β-strand	95	1	1
β-strand	103	1	1
α-helix	106	1
β-strand	107-111	5	1
β-strand	115-118	4	1
β-strand	121-127	7	1
α-helix	128	1
β-strand	129-130	2	2
α-helix	131	1
β-strand	139-148	10	2
β-strand	156-160	5	1
β-strand	166	1	1
α-helix	170-173	4
β-strand	176-188	13	2
β-strand	189-190	2	3
β-strand	198-209	12	2

Chain C: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	4
β-strand	10-13	4	5
β-strand	19-25	7	4
β-strand	33-38	6	5
β-strand	45-49	5	5
β-strand	53-54	2	5
α-helix	55	1
β-strand	62-67	6	4
β-strand	70-75	6	4
β-strand	85-90	6	5
β-strand	96-97	2	5
β-strand	101-105	5	5
β-strand	110	1	6
α-helix	111-112	2
β-strand	113-117	5	7
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-138	11	7
β-strand	139	1	6
β-strand	143-149	7	8
β-strand	152-154	3	8
β-strand	158-162	5	7
α-helix	163-166	4
β-strand	172-181	10	7
α-helix	182-186	5
β-strand	190-197	8	8
β-strand	204-209	6	8

Chain D: 11 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	9
β-strand	11-12	2	10
β-strand	18-25	8	9
β-strand	33-40	8	5
β-strand	46-51	6	5
β-strand	57-59	3	5
α-helix	61-66	6
β-strand	67-72	6	9
α-helix	73-75	3
β-strand	77-82	6	9
α-helix	87-89	3
β-strand	91-101	11	5
β-strand	104-110	7	5
β-strand	114-116	3	5
β-strand	117-118	2	10
α-helix	122-123	2
β-strand	124	1	11
α-helix	125-126	2
β-strand	127-131	5	12
β-strand	143-152	10	12
β-strand	153	1	11
β-strand	158-161	4	13
α-helix	167-169	3
β-strand	170-172	3	12
α-helix	173-175	3
β-strand	176-177	2	12
β-strand	182-190	9	12
α-helix	194-197	4
α-helix	199-200	2
β-strand	201-206	6	13
α-helix	207-209	3
β-strand	211-216	6	13
α-helix	217-218	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholine receptor subunit alpha 1	B	protein	212	Homo sapiens	P02708 (AlphaFold model)
Fab35, Light Chain	C	protein	213	Rattus norvegicus
Fab35, Heavy Chain	D	protein	219	Rattus norvegicus
Alpha-bungarotoxin isoform V31	A	protein	74	Bungarus multicinctus	P60616 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>5HBT_1 Acetylcholine receptor subunit alpha 1 (chains B)
KSEHETRLEAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQ
WVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWT
PPAIFKSYCEIIVTHFPFDEQNCSMKLGTRTYDGSAVAINPESDQPDLSNFMESGEWVIK
ESRGWKHSVTYSCCPDTPYLDITYHFVMQRLP

Sequence of entity 2 (C), FASTA

>5HBT_2 Fab35, Light Chain (chains C)
DIVITQSPSLLSASVGDRVTLTCKGSQNIDNYLAWYQQKLGEAPKLLIYKTNSLQTGIPS
RFSGSGSGTDYTLTISSLHSEDLATYYCYQYINGYTFGTGTKLELKRADAAPTVSIFPPS
TEQLATGGASVVCLMNNFYPRDISVKWKIDGTERRDGVLDSVTDQDSKDSTYSMSSTLSL
TKADYESHNLYTCEVVHKTSSSPVVKSFNRNEC

Sequence of entity 3 (D), FASTA

>5HBT_3 Fab35, Heavy Chain (chains D)
EVQLQESGPGLVQPSETLSLTCTVSGFSLTSYSVSWLRQPSGKGPEWMGRMWDDGGTVYN
SGLKSRLSISRDTSKNQVFLKMNSLQTDDTGTYYCTRDERIRAINWFAYWGQGTLVTVSS
AETTAPSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSG
LYTLTSSVTVPSSTWPSQTVTCNVAHPGQQHQRWTRKLC

Sequence of entity 4 (A), FASTA

>5HBT_4 Alpha-bungarotoxin isoform V31 (chains A)
IVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCC
STDKCNPHPKQRPG

Primary citation

Structural insights into the molecular mechanisms of myasthenia gravis and their therapeutic implications. Noridomi, K., Watanabe, G., Hansen, M.N. et al. Elife (2017) 6. DOI 10.7554/eLife.23043 · 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
4ZJS 2.23 Å, Crystal structure of a chimeric acetylcholine binding protein from Aplysia Californica…
9DML 2.24 Å, Human muscle nAChR with fab2-bound
9YEI 2.36 Å, Human muscle nAChR SCCMS eL269F ACh, Reboxetine bound (lower 1)

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