Peptide Information

General Information of This Peptide
Peptide ID
BTDP007777
Peptide Name
Acetylcholinesterase
Symonym
BfAChE; EC 3.1.1.7
Species
Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
Uniprot Name
ACES_BUNFA
Alphafold ID
Q92035
3D Structure
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2D Sequence
3D Structure
Source
RSCB PDB: 4QWW
Sequence
MPSCQPGKMPAPWPWWLQLLLCIPSCVAVLPGRAGELKVSTQTGSVRGLSLPVLDGHVSA
FLGIPFAEPPLGRMRFLRPEPVKPWQHVLDATSYKPACYQMVDTSYPGFQGTEMWNPNRG
MSEDCLYLNIWVPSPRPKDAPVLVWIYGGGFYSGAASLDVYDGRFLTYTQNVILVSLSYR
VGAFGFLGLPGSPEAPGNMGLLDQRLALQWIQNNIHPFGGNPRAVTVFGESAGAASVGMH
LLSTQSRTLFQRAILQSGGPNAPWATVTPAESRGRAALLGKQLGCHFNNDSELVSCLRSK
NPQELIDEEWSVLPYKSIFRFPFVPVIDGDFFPDTPEAMLSSGNFKETQVLLGVVKDEGS
YFLIYGLPGFSKDNESLISRADFLEGVRMSVPHANDIATDAVVLQYTDWQDQDNREKNRE
ALDDIVGDHNVICPVVQFANDYAKRNSKVYAYLFDHRASNLLWPPWMGVPHGYEIEFVFG
LPLNDSLNYTPQEKELSRRMMRYWANFARTGNPTDPADKSGAWPTYTASQPQYVQLNTQP
LATQPSLRAQICAFWNHFLPKLLNATDNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQ
DRCSEL
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Sequence Length
606
Mass (Da)
68074
Sequence Removed Signal Peptide
MPSCQPGKMPAPWPWWLQLLLCIPSCVAVLPGRAGELKVSTQTGSVRGLSLPVLDGHVSA
FLGIPFAEPPLGRMRFLRPEPVKPWQHVLDATSYKPACYQMVDTSYPGFQGTEMWNPNRG
MSEDCLYLNIWVPSPRPKDAPVLVWIYGGGFYSGAASLDVYDGRFLTYTQNVILVSLSYR
VGAFGFLGLPGSPEAPGNMGLLDQRLALQWIQNNIHPFGGNPRAVTVFGESAGAASVGMH
LLSTQSRTLFQRAILQSGGPNAPWATVTPAESRGRAALLGKQLGCHFNNDSELVSCLRSK
NPQELIDEEWSVLPYKSIFRFPFVPVIDGDFFPDTPEAMLSSGNFKETQVLLGVVKDEGS
YFLIYGLPGFSKDNESLISRADFLEGVRMSVPHANDIATDAVVLQYTDWQDQDNREKNRE
ALDDIVGDHNVICPVVQFANDYAKRNSKVYAYLFDHRASNLLWPPWMGVPHGYEIEFVFG
LPLNDSLNYTPQEKELSRRMMRYWANFARTGNPTDPADKSGAWPTYTASQPQYVQLNTQP
LATQPSLRAQICAFWNHFLPKLLNATDNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQ
DRCSEL
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Disulfide Bond
98-125;285-296;433-552;603
PDB ID
4QWW
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Lepidosauria
Order: Squamata
Family: Elapidae
Genus: Bungarus
Species: Bungarus fasciatus
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
References
Ref 1 Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of cooh-terminal domain; involvement of a positively charged residue in the peripheral site. J Biol Chem. 1996 Jun 21;271(25):15099-108. doi: 10.1074/jbc.271.25.15099.
Ref 2 Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle. J Biol Chem. 1998 Apr 17;273(16):9812-20. doi: 10.1074/jbc.273.16.9812.
Ref 3 Acetylcholinesterase from Bungarus venom: a monomeric species. FEBS Lett. 1996 Jun 3;387(2-3):196-200. doi: 10.1016/0014-5793(96)00447-4.
Ref 4 The acetylcholinesterase of Bungarus fasciatus venom. Eur J Biochem. 1973 May 2;34(3):586-92. doi: 10.1111/j.1432-1033.1973.tb02799.x.
Ref 5 Acetylcholinesterases from Elapidae snake venoms: biochemical, immunological and enzymatic characterization. Biochim Biophys Acta. 1997 May 23;1339(2):253-67. doi: 10.1016/s0167-4838(97)00009-5.
Ref 6 Crystal structure of snake venom acetylcholinesterase in complex with inhibitory antibody fragment Fab410 bound at the peripheral site: evidence for open and closed states of a back door channel. J Biol Chem. 2015 Jan 16;290(3):1522-35. doi: 10.1074/jbc.M114.603902. Epub 2014 Nov 19.
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