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1MAH

FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0001919biological_processregulation of receptor recycling
A0002076biological_processosteoblast development
A0003990molecular_functionacetylcholinesterase activity
A0004104molecular_functioncholinesterase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005635cellular_componentnuclear envelope
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006581biological_processacetylcholine catabolic process
A0007155biological_processcell adhesion
A0007416biological_processsynapse assembly
A0008291biological_processacetylcholine metabolic process
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017171molecular_functionserine hydrolase activity
A0019695biological_processcholine metabolic process
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0031594cellular_componentneuromuscular junction
A0031623biological_processreceptor internalization
A0032868biological_processresponse to insulin
A0042166molecular_functionacetylcholine binding
A0042734cellular_componentpresynaptic membrane
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043025cellular_componentneuronal cell body
A0043083cellular_componentsynaptic cleft
A0043236molecular_functionlaminin binding
A0045121cellular_componentmembrane raft
A0045202cellular_componentsynapse
A0045211cellular_componentpostsynaptic membrane
A0048471cellular_componentperinuclear region of cytoplasm
A0050772biological_processpositive regulation of axonogenesis
A0050775biological_processpositive regulation of dendrite morphogenesis
A0052689molecular_functioncarboxylic ester hydrolase activity
A0060041biological_processretina development in camera-type eye
A0095500biological_processacetylcholine receptor signaling pathway
A0098552cellular_componentside of membrane
A0120162biological_processpositive regulation of cold-induced thermogenesis
F0005576cellular_componentextracellular region
F0035821biological_processmodulation of process of another organism
F0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idCAT
Number of Residues4
DetailsLOCATED AT THE BOTTOM OF A NARROW GORGE
ChainResidue
ASER203
AGLU334
AHIS447
ATRP86

site_idPAS
Number of Residues4
DetailsBINDING SITE FOR FAS2 LOOP II
ChainResidue
ATYR72
ATYR124
AGLN279
ATYR341

Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpmsVtLfGeSAG
ChainResidueDetails
APHE190-GLY205

site_idPS00272
Number of Residues19
DetailsSNAKE_TOXIN Snake toxins signature. GCg..CPpgddnlevk.CCtsP
ChainResidueDetails
FGLY38-PRO56

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP
ChainResidueDetails
AGLU94-PRO104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Acyl-ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Blocks the entrance of the active site gorge of hAChE","evidences":[{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
AGLU334
AHIS447
ASER203

246333

PDB entries from 2025-12-17

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