5HBV: Alpha-bungarotoxin isoform V31

Complex structure of Fab35 and mouse nAChR alpha1. Determined by X-ray diffraction at 2.7 Å resolution. Released 3 May 2017.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Bungarus multicinctus, Mus musculus, Rattus norvegicus
Chains: 4
Atoms: 5,705
Mol. weight: 81.59 kDa
Released: 3 May 2017

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

Secondary structure: helices and β-sheets

5HBV contains 22 α-helices and 62 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: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	1
β-strand	12-15	4	1
α-helix	16-17	2
β-strand	22-28	7	2
α-helix	33-36	4
β-strand	39-45	7	2
α-helix	48-51	4
β-strand	56-60	5	2

Chain B: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	1-12	12
α-helix	27-28	2
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	90-93	4	2
α-helix	101-102	2
β-strand	103	1	3
α-helix	106	1
β-strand	107-111	5	3
β-strand	113-118	6	3
β-strand	121-127	7	3
β-strand	128-130	3	2
α-helix	131	1
β-strand	139-148	10	2
β-strand	156-160	5	3
β-strand	166	1	3
β-strand	176-190	15	2
β-strand	193-209	17	2

Chain C: 7 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
α-helix	80-82	3
β-strand	85-90	6	5
β-strand	96-97	2	5
β-strand	101-105	5	5
β-strand	110	1	6
β-strand	113-117	5	7
α-helix	118-120	3
α-helix	121-125	5
β-strand	129-138	10	7
β-strand	139	1	6
β-strand	143-149	7	8
β-strand	152-153	2	8
β-strand	158-162	5	7
α-helix	163-164	2
β-strand	172-180	9	7
α-helix	182-186	5
β-strand	191-197	7	8
α-helix	203	1
β-strand	204-208	5	8

Chain D: 5 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	11
β-strand	46-51	6	11
β-strand	57-59	3	11
α-helix	61-63	3
β-strand	67-72	6	9
β-strand	77-82	6	9
α-helix	87-89	3
β-strand	91-101	11	11
β-strand	104-110	7	11
β-strand	115-116	2	11
β-strand	117-118	2	10
β-strand	124	1	12
α-helix	125-126	2
β-strand	127-131	5	13
β-strand	143-152	10	13
β-strand	153	1	12
β-strand	158-161	4	14
α-helix	167-169	3
β-strand	170-172	3	13
β-strand	176-177	2	13
β-strand	182-190	9	13
α-helix	194-197	4
β-strand	201-206	6	14
β-strand	211-216	6	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-bungarotoxin isoform V31	A	protein	74	Bungarus multicinctus	P60616 (AlphaFold model)
Acetylcholine receptor subunit alpha 1	B	protein	212	Mus musculus	P04756 (AlphaFold model)
Fab35, Light Chain	C	protein	213	Rattus norvegicus
Fab35, Heavy Chain	D	protein	219	Rattus norvegicus

Sequence of entity 1 (A), FASTA

>5HBV_1 Alpha-bungarotoxin isoform V31 (chains A)
IVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCC
STDKCNPHPKQRPG

Sequence of entity 2 (B), FASTA

>5HBV_2 Acetylcholine receptor subunit alpha 1 (chains B)
KSEHETRLEAKLFEDYSSVVRPVEDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQ
WVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWT
PPAIFKSYCEIIVTHFPFDEQNCSMKLGTRTYDGSAVAINPESDQPDLSNFMESGEWVIK
EARGWKHWVFYSCCPTTPYLDITYHFVMQRLP

Sequence of entity 3 (C), FASTA

>5HBV_3 Fab35, Light Chain (chains C)
DIVITQSPSLLSASVGDRVTLTCKGSQNIDNYLAWYQQKLGEAPKLLIYKTNSLQTGIPS
RFSGSGSGTDYTLTISSLHSEDLATYYCYQYINGYTFGTGTKLELKRADAAPTVSIFPPS
TEQLATGGASVVCLMNNFYPRDISVKWKIDGTERRDGVLDSVTDQDSKDSTYSMSSTLSL
TKADYESHNLYTCEVVHKTSSSPVVKSFNRNEC

Sequence of entity 4 (D), FASTA

>5HBV_4 Fab35, Heavy Chain (chains D)
EVQLQESGPGLVQPSETLSLTCTVSGFSLTSYSVSWLRQPSGKGPEWMGRMWDDGGTVYN
SGLKSRLSISRDTSKNQVFLKMNSLQTDDTGTYYCTRDERIRAINWFAYWGQGTLVTVSS
AETTAPSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVLQSG
LYTLTSSVTVPSSTWPSQTVTCNVAHPGQQHQRWTRKLC

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 P60616 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1HC9 1.8 Å, alpha-bungarotoxin complexed with high affinity peptide
2QC1 1.94 Å, Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1…
5HBT 2.61 Å, Complex structure of Fab35 and human nAChR alpha1
4UY2 2.7 Å, Crystal structure of the complex of the extracellular domain of human alpha9 nAChR with…
7KOO 3.0 Å, Alpha-7 nicotinic acetylcholine receptor bound to alpha-bungarotoxin in a resting state
4HQP 3.51 Å, Alpha7 nicotinic receptor chimera and its complex with Alpha bungarotoxin

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