1Z0H: Botulinum neurotoxin type B

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Mar 2005.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Clostridium botulinum
Chains: 2
Atoms: 7,864
Mol. weight: 105.46 kDa
Released: 15 Mar 2005

Explore 1Z0H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z0H contains 18 α-helices and 92 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: 10 helices, 44 β-strands

Element	Residues	Length	Sheet
α-helix	858-860	3
β-strand	863-866	4	1
β-strand	867-869	3	2
β-strand	874-876	3	2
β-strand	883-886	4	3
β-strand	891-892	2	1
β-strand	897-900	4	1
β-strand	908-911	4	3
β-strand	921-922	2	4
β-strand	925-932	8	1
α-helix	933-937	5
α-helix	938-940	3
α-helix	941-946	6
β-strand	948-956	9	3
β-strand	959-966	8	3
β-strand	969-975	7	3
β-strand	981-987	7	3
β-strand	1002-1008	7	1
β-strand	1012-1017	6	1
β-strand	1020-1026	7	1
β-strand	1033-1034	2	4
β-strand	1038-1044	7	3
β-strand	1053-1061	9	1
α-helix	1067-1078	12
β-strand	1082	1	5
β-strand	1084	1	6
β-strand	1090	1	6
α-helix	1091	1
β-strand	1092-1093	2	7
β-strand	1096-1101	6	8
α-helix	1102-1104	3
β-strand	1107-1111	5	8
α-helix	1112	1
β-strand	1118-1122	5	8
α-helix	1123-1124	2
β-strand	1125	1	9
β-strand	1136	1	9
β-strand	1143-1148	6	8
β-strand	1158-1159	2	7
β-strand	1161	1	5
β-strand	1165-1172	8	8
β-strand	1175-1180	6	8
β-strand	1181-1182	2	10
β-strand	1189-1191	3	8
β-strand	1193-1196	4	8
β-strand	1203-1204	2	10
β-strand	1207-1210	4	8
β-strand	1220-1225	6	8
β-strand	1233-1244	12	8
β-strand	1251-1259	9	8
α-helix	1260-1265	6
β-strand	1279-1282	4	8
β-strand	1285	1	11
β-strand	1288	1	11

Chain B: 8 helices, 48 β-strands

Element	Residues	Length	Sheet
α-helix	855-860	6
β-strand	863-866	4	12
β-strand	867-869	3	13
β-strand	874-876	3	13
β-strand	883-886	4	14
β-strand	891-892	2	12
β-strand	897-901	5	12
β-strand	908-911	4	14
β-strand	921	1	15
β-strand	925-932	8	12
α-helix	933-937	5
α-helix	941-946	6
β-strand	948-956	9	14
β-strand	959-966	8	14
β-strand	969-975	7	14
β-strand	981-987	7	14
β-strand	991	1	16
β-strand	1002-1008	7	12
β-strand	1012-1017	6	12
β-strand	1020-1026	7	12
β-strand	1034	1	15
β-strand	1038-1044	7	14
β-strand	1052-1061	10	12
α-helix	1067-1078	12
β-strand	1082	1	17
β-strand	1084	1	18
β-strand	1090	1	18
α-helix	1091	1
β-strand	1092-1093	2	19
β-strand	1096-1097	2	20
β-strand	1098-1101	4	21
α-helix	1102-1104	3
β-strand	1107-1111	5	20
β-strand	1118-1122	5	20
α-helix	1123-1124	2
β-strand	1125	1	22
β-strand	1134	1	16
β-strand	1136	1	22
β-strand	1143-1148	6	20
β-strand	1158-1159	2	19
β-strand	1161	1	17
β-strand	1165-1172	8	20
β-strand	1175-1180	6	20
β-strand	1181-1182	2	23
β-strand	1189-1191	3	20
β-strand	1193-1196	4	20
β-strand	1203-1204	2	23
β-strand	1207-1210	4	20
β-strand	1220	1	21
β-strand	1221-1225	5	20
β-strand	1233-1245	13	20
β-strand	1250-1259	10	20
α-helix	1262-1265	4
β-strand	1279-1282	4	21
β-strand	1285	1	24
β-strand	1288	1	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Botulinum neurotoxin type B	A, B	protein	438	Clostridium botulinum	P10844 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1Z0H_1 Botulinum neurotoxin type B (chains A, B)
NKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQ
NQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIW
TLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIRE
VIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLM
YNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNS
QSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEY
DEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYN
LKLGCNWQFIPKDEGWTE

Primary citation

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B. Jayaraman, S., Eswaramoorthy, S., Ahmed, S.A. et al. Biochem Biophys Res Commun (2005) 330:97-103. DOI 10.1016/j.bbrc.2005.02.123 · PubMed

Other PDB entries of the same protein (UniProt P10844 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7NA9 1.76 Å, Crystal structure of BoNT/B-LC-JSG-C1
1EPW 1.9 Å, Crystal structure of clostridium neurotoxin type B
1S0E 1.9 Å, Crystal structure of botulinum neurotoxin type B at pH 6.0
5VMR 1.95 Å, Receptor binding domain of BoNT/B in complex with mini-protein binder Bot.2110.4
1G9B 2.0 Å, Crystal structure of clostridium botulinum neurotoxin B complexed with an inhibitor…
1S0B 2.0 Å, Crystal structure of botulinum neurotoxin type B at pH 4.0
6G5G 2.0 Å, Crystal structure of an engineered Botulinum Neurotoxin type B mutant E1191M/S1199Y in…
6G5K 2.0 Å, Crystal structure of the binding domain of Botulinum Neurotoxin type B in complex with…
1G9A 2.1 Å, Crystal structure of clostridium botulinum neurotoxin B complexed with an inhibitor…
2NM1 2.15 Å, Structure of BoNT/B in complex with its protein receptor
1F82 2.2 Å, Botulinum neurotoxin type B catalytic domain
1G9D 2.2 Å, Crystal structure of clostridium botulinum neurotoxin B complexed with an inhibitor…

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