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Botulinum neurotoxin type A (BoNT/A) (EC 3.4.24.69) (Bontoxilysin-A) (BOTOX) [Cleaved into: Botulinum neurotoxin A light chain; Botulinum neurotoxin A heavy chain]

 BXA1_CLOBO              Reviewed;        1296 AA.
P10845; P01561; P18639;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-JUN-2018, entry version 197.
RecName: Full=Botulinum neurotoxin type A;
Short=BoNT/A;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-A;
Short=BOTOX;
Contains:
RecName: Full=Botulinum neurotoxin A light chain;
Contains:
RecName: Full=Botulinum neurotoxin A heavy chain;
Flags: Precursor;
Name=botA; Synonyms=atx, bna;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NCTC 2916 / Type A;
PubMed=2185020; DOI=10.1111/j.1432-1033.1990.tb15461.x;
Thompson D.E., Brehm J.K., Oultram J.D., Swinfield T.-J., Shone C.C.,
Atkinson T., Melling J., Minton N.P.;
"The complete amino acid sequence of the Clostridium botulinum type A
neurotoxin, deduced by nucleotide sequence analysis of the encoding
gene.";
Eur. J. Biochem. 189:73-81(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=62A / Type A;
PubMed=2160960;
Binz T., Kurazono H., Wille M., Frevert J., Wernars K., Niemann H.;
"The complete sequence of botulinum neurotoxin type A and comparison
with other clostridial neurotoxins.";
J. Biol. Chem. 265:9153-9158(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
STRAIN=62A / Type A;
PubMed=8863443; DOI=10.1099/00207713-46-4-1105;
East A.K., Bhandari M., Stacey J.M., Campbell K.D., Collins M.D.;
"Organization and phylogenetic interrelationships of genes encoding
components of the botulinum toxin complex in proteolytic Clostridium
botulinum types A, B, and F: evidence of chimeric sequences in the
gene encoding the nontoxic nonhemagglutinin component.";
Int. J. Syst. Bacteriol. 46:1105-1112(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
STRAIN=NIH / Type A;
PubMed=8521962; DOI=10.1016/0014-5793(95)01241-5;
Fujita R., Fujinaga Y., Inoue K., Nakajima H., Kumon H., Oguma K.;
"Molecular characterization of two forms of nontoxic-nonhemagglutinin
components of Clostridium botulinum type A progenitor toxins.";
FEBS Lett. 376:41-44(1995).
[5]
PROTEIN SEQUENCE OF 2-17.
PubMed=6370252; DOI=10.1016/0006-291X(84)90858-1;
Schmidt J.J., Sartymoorthy V., Dasgupta B.R.;
"Partial amino acid sequence of the heavy and light chains of
botulinum neurotoxin type A.";
Biochem. Biophys. Res. Commun. 119:900-904(1984).
[6]
PROTEIN SEQUENCE OF 2-47.
Dasgupta B.R., Foley J., Niece R.;
"Partial sequence of the light chain of botulinum neurotoxin type A.";
Biochemistry 26:4162-4162(1987).
[7]
PROTEIN SEQUENCE OF 2-6 AND 445-457.
PubMed=2126206; DOI=10.1016/0300-9084(90)90048-L;
Dasgupta B.R., Dekleva M.L.;
"Botulinum neurotoxin type A: sequence of amino acids at the N-
terminus and around the nicking site.";
Biochimie 72:661-664(1990).
[8]
PROTEIN SEQUENCE OF 449-475 AND 873-896.
PubMed=3178218; DOI=10.1016/0003-9861(88)90244-5;
Sathymoorthy V., Dasgupta B.R., Foley J., Niece R.L.;
"Botulinum neurotoxin type A: cleavage of the heavy chain into two
halves and their partial sequences.";
Arch. Biochem. Biophys. 266:142-151(1988).
[9]
PROTEIN SEQUENCE OF 449-483.
PubMed=3896784; DOI=10.1111/j.1432-1033.1985.tb09070.x;
Shone C.C., Hambleton P., Melling J.;
"Inactivation of Clostridium botulinum type A neurotoxin by trypsin
and purification of two tryptic fragments. Proteolytic action near the
COOH-terminus of the heavy subunit destroys toxin-binding activity.";
Eur. J. Biochem. 151:75-82(1985).
[10]
IDENTIFICATION OF SUBSTRATE.
PubMed=8243676; DOI=10.1016/0014-5793(93)80448-4;
Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J.,
Benfenati F., Wilson M.C., Montecucco C.;
"Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct
COOH-terminal peptide bonds.";
FEBS Lett. 335:99-103(1993).
[11]
MUTAGENESIS OF GLU-262; PHE-266 AND TYR-366.
PubMed=11700044; DOI=10.1006/bbrc.2001.5911;
Rigoni M., Caccin P., Johnson E.A., Montecucco C., Rossetto O.;
"Site-directed mutagenesis identifies active-site residues of the
light chain of botulinum neurotoxin type a.";
Biochem. Biophys. Res. Commun. 288:1231-1237(2001).
[12]
INTERACTION WITH SV2.
PubMed=16543415; DOI=10.1126/science.1123654;
Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R.,
Chapman E.R.;
"SV2 is the protein receptor for botulinum neurotoxin A.";
Science 312:592-596(2006).
[13]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
PubMed=9783750; DOI=10.1038/2338;
Lacy D.B., Tepp W., Cohen A.C., Dasgupta B.R., Stevens R.C.;
"Crystal structure of botulinum neurotoxin type A and implications for
toxicity.";
Nat. Struct. Biol. 5:898-902(1998).
-!- FUNCTION: Inhibits acetylcholine release. The botulinum toxin
binds with high affinity to peripheral neuronal presynaptic
membrane to the secretory vesicle protein SV2. It binds directly
to the largest luminal loop of SV2A, SV2B and SV2C. It is then
internalized by receptor-mediated endocytosis. The C-terminus of
the heavy chain (H) is responsible for the adherence of the toxin
to the cell surface while the N-terminus mediates transport of the
light chain from the endocytic vesicle to the cytosol. After
translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-
198 bond in SNAP-25, thereby blocking neurotransmitter release.
Inhibition of acetylcholine release results in flaccid paralysis,
with frequent heart or respiratory failure.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Disulfide-linked heterodimer of a light chain (L) and a
heavy chain (H).
-!- INTERACTION:
Q02563:Sv2a (xeno); NbExp=2; IntAct=EBI-8178893, EBI-466194;
Q496J9:SV2C (xeno); NbExp=4; IntAct=EBI-8178893, EBI-16081469;
Q9Z2I6:Sv2c (xeno); NbExp=12; IntAct=EBI-8178893, EBI-8178859;
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin A light chain:
Secreted. Host cytoplasm, host cytosol.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin A heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- PHARMACEUTICAL: Available under the name BOTOX (Allergan) for the
treatment of strabismus and blepharospasm associated with dystonia
and cervical dystonia. Also used for the treatment of hemifacial
spasm and a number of other neurological disorders characterized
by abnormal muscle contraction.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BOTOX product information Web site;
URL="http://www.botox.com/";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=From sausages to
wrinkles - Issue 19 of February 2002;
URL="https://web.expasy.org/spotlight/back_issues/019";
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
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EMBL; X52066; CAA36289.1; -; Genomic_DNA.
EMBL; M30196; AAA23262.1; -; Genomic_DNA.
EMBL; X92973; CAA63551.1; -; Genomic_DNA.
EMBL; D67030; BAA11051.1; -; Genomic_DNA.
EMBL; M27892; AAA23269.1; -; Genomic_DNA.
PIR; A35294; BTCLAB.
RefSeq; WP_003356619.1; NZ_LFOS01000037.1.
RefSeq; WP_011948511.1; NZ_LHUL01000004.1.
PDB; 1UEE; Model; -; A=2-545.
PDB; 1XTF; X-ray; 2.20 A; A/B=2-420.
PDB; 1XTG; X-ray; 2.10 A; A=2-420.
PDB; 2ILP; X-ray; 1.90 A; A/B=3-424.
PDB; 2IMA; X-ray; 1.94 A; A/B=1-424.
PDB; 2IMB; X-ray; 2.41 A; A/B=3-424.
PDB; 2IMC; X-ray; 2.00 A; A/B=3-424.
PDB; 2ISE; X-ray; 2.20 A; A/B=1-420.
PDB; 2ISG; X-ray; 2.00 A; A/B=1-420.
PDB; 2ISH; X-ray; 2.00 A; A/B=1-420.
PDB; 2NYY; X-ray; 2.61 A; A=2-1296.
PDB; 2NZ9; X-ray; 3.79 A; A/B=2-1296.
PDB; 2VU9; X-ray; 1.60 A; A=876-1296.
PDB; 2VUA; X-ray; 1.70 A; A=876-1296.
PDB; 2W2D; X-ray; 2.59 A; A/C=3-442, B/D=447-877.
PDB; 3BOK; X-ray; 1.25 A; A=3-425.
PDB; 3BON; X-ray; 1.20 A; A=3-425.
PDB; 3BOO; X-ray; 1.40 A; A=3-425.
PDB; 3BTA; X-ray; 3.20 A; A=2-1296.
PDB; 3BWI; X-ray; 1.70 A; A=1-424.
PDB; 3C88; X-ray; 1.60 A; A=1-424.
PDB; 3C89; X-ray; 1.58 A; A=1-424.
PDB; 3C8A; X-ray; 1.52 A; A=1-424.
PDB; 3C8B; X-ray; 1.47 A; A=1-424.
PDB; 3DDA; X-ray; 1.50 A; A=1-424.
PDB; 3DDB; X-ray; 1.60 A; A=1-424.
PDB; 3DS9; X-ray; 1.76 A; A=1-417.
PDB; 3FUO; X-ray; 1.80 A; A=871-1296.
PDB; 3V0A; X-ray; 2.70 A; A=1-1296.
PDB; 3V0B; X-ray; 3.90 A; A=1-1296.
PDB; 3V0C; X-ray; 4.30 A; A=1-1296.
PDB; 3ZUR; X-ray; 2.71 A; A/B=3-430, A/B=454-865.
PDB; 3ZUS; X-ray; 2.95 A; A/B/C/D=3-431, A/B/C/D=454-865.
PDB; 4EJ5; X-ray; 1.87 A; A=1-425.
PDB; 4EL4; X-ray; 1.20 A; A=1-425.
PDB; 4ELC; X-ray; 1.80 A; A=1-425.
PDB; 4HEV; X-ray; 2.50 A; A/B=1-425.
PDB; 4IQP; X-ray; 2.30 A; A=871-1296.
PDB; 4JRA; X-ray; 2.30 A; A/B=871-1296.
PDB; 4ZJX; X-ray; 1.94 A; A=1-424.
PDB; 5JLV; X-ray; 2.00 A; A/B=872-1296.
PDB; 5JMC; X-ray; 2.64 A; A/C/E/G=872-1296.
PDB; 5MK6; X-ray; 1.45 A; A=871-1296.
PDB; 5MK7; X-ray; 1.80 A; A=871-1296.
PDB; 5TPB; X-ray; 2.60 A; A/B=876-1296.
PDB; 5TPC; X-ray; 2.00 A; A=876-1296.
PDB; 5V8P; X-ray; 2.50 A; A/B=1-424.
PDB; 5V8R; X-ray; 1.90 A; A/B=1-424.
PDB; 5V8U; X-ray; 2.05 A; A/B=1-424.
PDB; 5VGV; X-ray; 2.60 A; A=1-425.
PDB; 5VGX; X-ray; 2.15 A; A=1-425.
PDBsum; 1UEE; -.
PDBsum; 1XTF; -.
PDBsum; 1XTG; -.
PDBsum; 2ILP; -.
PDBsum; 2IMA; -.
PDBsum; 2IMB; -.
PDBsum; 2IMC; -.
PDBsum; 2ISE; -.
PDBsum; 2ISG; -.
PDBsum; 2ISH; -.
PDBsum; 2NYY; -.
PDBsum; 2NZ9; -.
PDBsum; 2VU9; -.
PDBsum; 2VUA; -.
PDBsum; 2W2D; -.
PDBsum; 3BOK; -.
PDBsum; 3BON; -.
PDBsum; 3BOO; -.
PDBsum; 3BTA; -.
PDBsum; 3BWI; -.
PDBsum; 3C88; -.
PDBsum; 3C89; -.
PDBsum; 3C8A; -.
PDBsum; 3C8B; -.
PDBsum; 3DDA; -.
PDBsum; 3DDB; -.
PDBsum; 3DS9; -.
PDBsum; 3FUO; -.
PDBsum; 3V0A; -.
PDBsum; 3V0B; -.
PDBsum; 3V0C; -.
PDBsum; 3ZUR; -.
PDBsum; 3ZUS; -.
PDBsum; 4EJ5; -.
PDBsum; 4EL4; -.
PDBsum; 4ELC; -.
PDBsum; 4HEV; -.
PDBsum; 4IQP; -.
PDBsum; 4JRA; -.
PDBsum; 4ZJX; -.
PDBsum; 5JLV; -.
PDBsum; 5JMC; -.
PDBsum; 5MK6; -.
PDBsum; 5MK7; -.
PDBsum; 5TPB; -.
PDBsum; 5TPC; -.
PDBsum; 5V8P; -.
PDBsum; 5V8R; -.
PDBsum; 5V8U; -.
PDBsum; 5VGV; -.
PDBsum; 5VGX; -.
ProteinModelPortal; P10845; -.
SMR; P10845; -.
DIP; DIP-42781N; -.
IntAct; P10845; 4.
MINT; P10845; -.
BindingDB; P10845; -.
ChEMBL; CHEMBL5192; -.
DrugBank; DB07819; (2E)-3-(4-CHLOROPHENYL)-N-HYDROXYACRYLAMIDE.
Allergome; 12104; Clo bo Toxin.
TCDB; 1.C.8.1.1; the botulinum and tetanus toxin (btt) family.
PRIDE; P10845; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250968; Toxicity of botulinum toxin type A (BoNT/A).
EvolutionaryTrace; P10845; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0044156; C:host cell junction; IEA:UniProtKB-KW.
GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:1905576; F:ganglioside GT1b binding; IDA:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; EXP:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:InterPro.
Gene3D; 1.20.1120.10; -; 1.
InterPro; IPR000395; Bot/tetX_LC.
InterPro; IPR036248; Clostridium_toxin_transloc.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR013104; Toxin_rcpt-bd_C.
InterPro; IPR012928; Toxin_rcpt-bd_N.
InterPro; IPR012500; Toxin_trans.
Pfam; PF01742; Peptidase_M27; 1.
Pfam; PF07951; Toxin_R_bind_C; 1.
Pfam; PF07953; Toxin_R_bind_N; 1.
Pfam; PF07952; Toxin_trans; 1.
PRINTS; PR00760; BONTOXILYSIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50386; SSF50386; 1.
SUPFAM; SSF58091; SSF58091; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Host cell junction; Host cell membrane; Host cytoplasm; Host membrane;
Host synapse; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Neurotoxin; Pharmaceutical; Protease; Secreted; Toxin; Transmembrane;
Transmembrane helix; Virulence; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2126206,
ECO:0000269|PubMed:6370252,
ECO:0000269|Ref.6}.
CHAIN 2 448 Botulinum neurotoxin A light chain.
/FTId=PRO_0000029211.
CHAIN 449 1296 Botulinum neurotoxin A heavy chain.
/FTId=PRO_0000029212.
TRANSMEM 627 647 Helical. {ECO:0000255}.
TRANSMEM 656 676 Helical. {ECO:0000255}.
ACT_SITE 224 224
METAL 223 223 Zinc; catalytic.
METAL 227 227 Zinc; catalytic.
METAL 262 262 Zinc; catalytic.
DISULFID 430 454 Interchain (between light and heavy
chains).
DISULFID 1235 1280
VARIANT 27 27 V -> A.
MUTAGEN 262 262 E->A: Drastic decrease in enzymatic
activity. {ECO:0000269|PubMed:11700044}.
MUTAGEN 266 266 F->A: Decreases enzymatic activity.
{ECO:0000269|PubMed:11700044}.
MUTAGEN 366 366 Y->A: Decreases enzymatic activity.
{ECO:0000269|PubMed:11700044}.
CONFLICT 2 2 P -> Q (in Ref. 1; CAA36289).
{ECO:0000305}.
CONFLICT 480 480 E -> P (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 876 876 T -> L (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 892 892 S -> K (in Ref. 8; AA sequence).
{ECO:0000305}.
STRAND 3 6 {ECO:0000244|PDB:3C8B}.
STRAND 16 23 {ECO:0000244|PDB:3BON}.
STRAND 26 28 {ECO:0000244|PDB:3DDA}.
STRAND 33 39 {ECO:0000244|PDB:3BON}.
STRAND 42 48 {ECO:0000244|PDB:3BON}.
STRAND 51 53 {ECO:0000244|PDB:3C88}.
HELIX 54 56 {ECO:0000244|PDB:3C8B}.
TURN 64 66 {ECO:0000244|PDB:3C8B}.
TURN 68 70 {ECO:0000244|PDB:3DS9}.
TURN 75 78 {ECO:0000244|PDB:3BON}.
HELIX 81 99 {ECO:0000244|PDB:3BON}.
HELIX 102 113 {ECO:0000244|PDB:3BON}.
STRAND 126 128 {ECO:0000244|PDB:3BON}.
HELIX 131 133 {ECO:0000244|PDB:3BON}.
STRAND 134 138 {ECO:0000244|PDB:3BON}.
STRAND 140 142 {ECO:0000244|PDB:2IMB}.
STRAND 144 148 {ECO:0000244|PDB:3BON}.
STRAND 150 155 {ECO:0000244|PDB:3BON}.
STRAND 158 161 {ECO:0000244|PDB:4HEV}.
STRAND 164 166 {ECO:0000244|PDB:3BON}.
TURN 170 172 {ECO:0000244|PDB:4ELC}.
TURN 175 177 {ECO:0000244|PDB:3BON}.
STRAND 178 180 {ECO:0000244|PDB:3V0A}.
STRAND 184 187 {ECO:0000244|PDB:3BON}.
STRAND 192 196 {ECO:0000244|PDB:3BON}.
HELIX 200 203 {ECO:0000244|PDB:3BON}.
HELIX 206 208 {ECO:0000244|PDB:2IMB}.
STRAND 210 214 {ECO:0000244|PDB:2ILP}.
HELIX 217 232 {ECO:0000244|PDB:3BON}.
STRAND 242 244 {ECO:0000244|PDB:3BON}.
HELIX 249 253 {ECO:0000244|PDB:3BON}.
STRAND 257 259 {ECO:0000244|PDB:3BON}.
HELIX 260 266 {ECO:0000244|PDB:3BON}.
HELIX 268 271 {ECO:0000244|PDB:3BON}.
HELIX 276 299 {ECO:0000244|PDB:3BON}.
STRAND 302 308 {ECO:0000244|PDB:3BON}.
HELIX 310 321 {ECO:0000244|PDB:3BON}.
STRAND 323 325 {ECO:0000244|PDB:1XTF}.
STRAND 327 329 {ECO:0000244|PDB:3BOO}.
STRAND 331 333 {ECO:0000244|PDB:1XTF}.
HELIX 335 347 {ECO:0000244|PDB:3BON}.
HELIX 351 358 {ECO:0000244|PDB:3BON}.
STRAND 366 368 {ECO:0000244|PDB:3BON}.
STRAND 372 375 {ECO:0000244|PDB:3BON}.
TURN 381 383 {ECO:0000244|PDB:3BON}.
TURN 386 388 {ECO:0000244|PDB:3BON}.
STRAND 393 395 {ECO:0000244|PDB:2IMB}.
HELIX 396 398 {ECO:0000244|PDB:3BOK}.
HELIX 399 401 {ECO:0000244|PDB:3ZUS}.
HELIX 402 404 {ECO:0000244|PDB:3BON}.
TURN 406 409 {ECO:0000244|PDB:3BON}.
HELIX 410 412 {ECO:0000244|PDB:3BON}.
STRAND 414 418 {ECO:0000244|PDB:3BON}.
TURN 420 422 {ECO:0000244|PDB:4ELC}.
STRAND 424 431 {ECO:0000244|PDB:2NYY}.
STRAND 454 458 {ECO:0000244|PDB:2NYY}.
HELIX 459 461 {ECO:0000244|PDB:2NYY}.
HELIX 468 470 {ECO:0000244|PDB:2NYY}.
STRAND 479 481 {ECO:0000244|PDB:2NYY}.
HELIX 496 503 {ECO:0000244|PDB:2NYY}.
STRAND 542 547 {ECO:0000244|PDB:2NYY}.
HELIX 550 555 {ECO:0000244|PDB:2NYY}.
STRAND 563 565 {ECO:0000244|PDB:2NYY}.
STRAND 570 573 {ECO:0000244|PDB:2NYY}.
STRAND 576 579 {ECO:0000244|PDB:2NYY}.
STRAND 581 583 {ECO:0000244|PDB:3V0A}.
HELIX 589 593 {ECO:0000244|PDB:2NYY}.
HELIX 600 602 {ECO:0000244|PDB:3V0A}.
HELIX 603 618 {ECO:0000244|PDB:2NYY}.
STRAND 625 629 {ECO:0000244|PDB:3V0A}.
HELIX 637 641 {ECO:0000244|PDB:2NYY}.
TURN 642 645 {ECO:0000244|PDB:2NYY}.
STRAND 648 650 {ECO:0000244|PDB:3BTA}.
HELIX 652 659 {ECO:0000244|PDB:2NYY}.
HELIX 661 663 {ECO:0000244|PDB:2NYY}.
STRAND 679 681 {ECO:0000244|PDB:2NYY}.
HELIX 688 720 {ECO:0000244|PDB:2NYY}.
HELIX 722 752 {ECO:0000244|PDB:2NYY}.
TURN 758 761 {ECO:0000244|PDB:2NYY}.
HELIX 766 799 {ECO:0000244|PDB:2NYY}.
HELIX 801 825 {ECO:0000244|PDB:2NYY}.
TURN 826 833 {ECO:0000244|PDB:2NYY}.
HELIX 834 845 {ECO:0000244|PDB:2NYY}.
HELIX 853 855 {ECO:0000244|PDB:2NYY}.
HELIX 860 871 {ECO:0000244|PDB:2NYY}.
HELIX 874 876 {ECO:0000244|PDB:5MK6}.
STRAND 878 884 {ECO:0000244|PDB:5MK6}.
STRAND 887 890 {ECO:0000244|PDB:5MK6}.
STRAND 897 900 {ECO:0000244|PDB:5MK6}.
STRAND 904 906 {ECO:0000244|PDB:5MK6}.
STRAND 908 910 {ECO:0000244|PDB:5MK7}.
STRAND 913 919 {ECO:0000244|PDB:5MK6}.
STRAND 924 927 {ECO:0000244|PDB:5MK6}.
HELIX 930 932 {ECO:0000244|PDB:5MK6}.
STRAND 935 938 {ECO:0000244|PDB:5MK6}.
STRAND 941 948 {ECO:0000244|PDB:5MK6}.
HELIX 955 957 {ECO:0000244|PDB:5MK6}.
STRAND 962 969 {ECO:0000244|PDB:5MK6}.
STRAND 972 979 {ECO:0000244|PDB:5MK6}.
STRAND 982 988 {ECO:0000244|PDB:5MK6}.
STRAND 990 992 {ECO:0000244|PDB:2NYY}.
STRAND 994 1000 {ECO:0000244|PDB:5MK6}.
STRAND 1003 1007 {ECO:0000244|PDB:5MK6}.
STRAND 1015 1021 {ECO:0000244|PDB:5MK6}.
STRAND 1025 1031 {ECO:0000244|PDB:5MK6}.
STRAND 1034 1040 {ECO:0000244|PDB:5MK6}.
STRAND 1051 1059 {ECO:0000244|PDB:5MK6}.
STRAND 1066 1077 {ECO:0000244|PDB:5MK6}.
HELIX 1081 1090 {ECO:0000244|PDB:5MK6}.
TURN 1091 1095 {ECO:0000244|PDB:3FUO}.
STRAND 1102 1104 {ECO:0000244|PDB:5MK6}.
STRAND 1106 1108 {ECO:0000244|PDB:5MK6}.
STRAND 1111 1118 {ECO:0000244|PDB:5MK6}.
STRAND 1122 1129 {ECO:0000244|PDB:5MK6}.
STRAND 1132 1137 {ECO:0000244|PDB:5MK6}.
STRAND 1142 1145 {ECO:0000244|PDB:5MK6}.
TURN 1146 1148 {ECO:0000244|PDB:5MK6}.
STRAND 1149 1152 {ECO:0000244|PDB:5MK6}.
STRAND 1160 1165 {ECO:0000244|PDB:5MK6}.
STRAND 1170 1173 {ECO:0000244|PDB:2VUA}.
STRAND 1179 1188 {ECO:0000244|PDB:5MK6}.
STRAND 1190 1195 {ECO:0000244|PDB:5MK6}.
STRAND 1199 1205 {ECO:0000244|PDB:5MK6}.
STRAND 1207 1209 {ECO:0000244|PDB:5MK6}.
HELIX 1211 1213 {ECO:0000244|PDB:5MK6}.
STRAND 1220 1226 {ECO:0000244|PDB:5MK6}.
STRAND 1228 1240 {ECO:0000244|PDB:5MK6}.
STRAND 1242 1244 {ECO:0000244|PDB:5JMC}.
STRAND 1246 1255 {ECO:0000244|PDB:5MK6}.
STRAND 1258 1264 {ECO:0000244|PDB:5MK6}.
HELIX 1266 1272 {ECO:0000244|PDB:5MK6}.
HELIX 1275 1277 {ECO:0000244|PDB:2VU9}.
TURN 1278 1280 {ECO:0000244|PDB:2VU9}.
STRAND 1282 1285 {ECO:0000244|PDB:5MK6}.
TURN 1289 1291 {ECO:0000244|PDB:5MK6}.
SEQUENCE 1296 AA; 149454 MW; B731EF5BA5E62FDA CRC64;
MPFVNKQFNY KDPVNGVDIA YIKIPNVGQM QPVKAFKIHN KIWVIPERDT FTNPEEGDLN
PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS TDLGRMLLTS IVRGIPFWGG
STIDTELKVI DTNCINVIQP DGSYRSEELN LVIIGPSADI IQFECKSFGH EVLNLTRNGY
GSTQYIRFSP DFTFGFEESL EVDTNPLLGA GKFATDPAVT LAHELIHAGH RLYGIAINPN
RVFKVNTNAY YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDIASTLNKA
KSIVGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT EDNFVKFFKV
LNRKTYLNFD KAVFKINIVP KVNYTIYDGF NLRNTNLAAN FNGQNTEINN MNFTKLKNFT
GLFEFYKLLC VRGIITSKTK SLDKGYNKAL NDLCIKVNNW DLFFSPSEDN FTNDLNKGEE
ITSDTNIEAA EENISLDLIQ QYYLTFNFDN EPENISIENL SSDIIGQLEL MPNIERFPNG
KKYELDKYTM FHYLRAQEFE HGKSRIALTN SVNEALLNPS RVYTFFSSDY VKKVNKATEA
AMFLGWVEQL VYDFTDETSE VSTTDKIADI TIIIPYIGPA LNIGNMLYKD DFVGALIFSG
AVILLEFIPE IAIPVLGTFA LVSYIANKVL TVQTIDNALS KRNEKWDEVY KYIVTNWLAK
VNTQIDLIRK KMKEALENQA EATKAIINYQ YNQYTEEEKN NINFNIDDLS SKLNESINKA
MININKFLNQ CSVSYLMNSM IPYGVKRLED FDASLKDALL KYIYDNRGTL IGQVDRLKDK
VNNTLSTDIP FQLSKYVDNQ RLLSTFTEYI KNIINTSILN LRYESNHLID LSRYASKINI
GSKVNFDPID KNQIQLFNLE SSKIEVILKN AIVYNSMYEN FSTSFWIRIP KYFNSISLNN
EYTIINCMEN NSGWKVSLNY GEIIWTLQDT QEIKQRVVFK YSQMINISDY INRWIFVTIT
NNRLNNSKIY INGRLIDQKP ISNLGNIHAS NNIMFKLDGC RDTHRYIWIK YFNLFDKELN
EKEIKDLYDN QSNSGILKDF WGDYLQYDKP YYMLNLYDPN KYVDVNNVGI RGYMYLKGPR
GSVMTTNIYL NSSLYRGTKF IIKKYASGNK DNIVRNNDRV YINVVVKNKE YRLATNASQA
GVEKILSALE IPDVGNLSQV VVMKSKNDQG ITNKCKMNLQ DNNGNDIGFI GFHQFNNIAK
LVASNWYNRQ IERSSRTLGC SWEFIPVDDG WGERPL


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