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2X8B

Crystal structure of human acetylcholinesterase inhibited by aged tabun and complexed with fasciculin-II

Functional Information from GO Data
ChainGOidnamespacecontents
A0001507biological_processacetylcholine catabolic process in synaptic cleft
A0001540molecular_functionamyloid-beta binding
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
A0005634cellular_componentnucleus
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006581biological_processacetylcholine catabolic process
A0007155biological_processcell adhesion
A0007399biological_processnervous system development
A0007416biological_processsynapse assembly
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017171molecular_functionserine hydrolase activity
A0031594cellular_componentneuromuscular junction
A0031623biological_processreceptor internalization
A0032223biological_processnegative regulation of synaptic transmission, cholinergic
A0042166molecular_functionacetylcholine binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042982biological_processamyloid precursor protein metabolic process
A0043083cellular_componentsynaptic cleft
A0043236molecular_functionlaminin binding
A0043621molecular_functionobsolete protein self-association
A0045202cellular_componentsynapse
A0048471cellular_componentperinuclear region of cytoplasm
A0050714biological_processpositive regulation of protein secretion
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
B0005576cellular_componentextracellular region
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG
ChainResidueDetails
APHE190-GLY205

site_idPS00272
Number of Residues19
DetailsSNAKE_TOXIN Snake toxins signature. GCg..CPpgddnlevk.CCtsP
ChainResidueDetails
BGLY38-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
DetailsSITE: Blocks the entrance of the active site gorge of hAChE => ECO:0000303|PubMed:23679855
ChainResidueDetails
BMET33

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AGLU334
AHIS447

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:4EY5
ChainResidueDetails
ATRP86
ATYR133
ATYR337

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:4BDT
ChainResidueDetails
AGLY122
ASEN203
ATRP439
AHIS447

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:4EY6
ChainResidueDetails
AGLU202

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7
ChainResidueDetails
AASN265

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11053835, ECO:0000269|PubMed:20408548, ECO:0000269|PubMed:23035744, ECO:0000269|PubMed:23679855, ECO:0007744|PDB:1B41, ECO:0007744|PDB:1F8U, ECO:0007744|PDB:2X8B, ECO:0007744|PDB:4BDT, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7, ECO:0007744|PDB:4EY8
ChainResidueDetails
AASN350

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY8
ChainResidueDetails
AASN464

220113

PDB entries from 2024-05-22

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