1MAH
FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B [auth F] | d1mahf_ | Small proteins | Snake toxin-like | Snake toxin-like | Snake venom toxins | Fasciculin | (Dendroaspis angusticeps ) [TaxId: 8618 ], | SCOPe (2.08) |
A | d1maha_ | Alpha and beta proteins (a/b) | alpha/beta-Hydrolases | alpha/beta-Hydrolases | Acetylcholinesterase-like | Acetylcholinesterase | house mouse (Mus musculus ) [TaxId: 10090 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B [auth F] | Toxin_TOLIP | e1mahF1 | A: few secondary structure elements | X: Snake toxin-like (From Topology) | H: Snake toxin-like (From Topology) | T: Snake toxin-like | F: Toxin_TOLIP | ECOD (1.6) |
A | COesterase | e1mahA1 | A: a/b three-layered sandwiches | X: alpha/beta-Hydrolases (From Topology) | H: alpha/beta-Hydrolases (From Topology) | T: alpha/beta-Hydrolases | F: COesterase | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
B [auth F] | 2.10.60.10 | Mainly Beta | Ribbon | CD59 | CD59 | CATH (4.3.0) |
A | 3.40.50.1820 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Alpha/Beta hydrolase fold, catalytic domain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
B [auth F] | PF21947 | Snake toxin cobra-type (Toxin_cobra-type) | Snake toxin cobra-type | - | Family |
PF00135 | Carboxylesterase family (COesterase) | Carboxylesterase family | - | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
B [auth F] | IPR018354 | Snake toxin, conserved site | Conserved Site |
B [auth F] | IPR045860 | Snake toxin-like superfamily | Homologous Superfamily |
B [auth F] | IPR054131 | Snake toxin cobra-type | Family |
IPR050654 | Acetylcholinesterase-related enzymes | Family | |
IPR000997 | Cholinesterase | Family | |
IPR002018 | Carboxylesterase, type B | Domain | |
IPR019819 | Carboxylesterase type B, conserved site | Conserved Site | |
IPR019826 | Carboxylesterase type B, active site | Active Site | |
IPR029058 | Alpha/Beta hydrolase fold | Homologous Superfamily | |
IPR014788 | Acetylcholinesterase, tetramerisation domain | Domain |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
acetylcholinesterase M-CSA #922 | This enzyme is found in, or attached to, cellular or basement membranes of presynaptic cholinergic neurons and postsynaptic cholinoceptive cells within the neuromuscular junction. Signal transmission at the neuromuscular junction involves the release of acylcholine, its interaction with the acycholine receptor and hydrolysis, all occuring in a period of a few milliseconds. Rapid hydrolysis of the newly released aceytlcholine is vital in order to prevent continuous firing of the nerve impulses [PMID:8161450]. | Defined by 8 residues: GLY:A-121GLY:A-122SER:A-203ALA:A-204PHE:A-295GLU:A-334PHE:A-338HIS:A-447 | EC: 3.1.1.7 (PDB Primary Data) |