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3ZLV

Crystal structure of mouse acetylcholinesterase in complex with tabun and HI-6

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
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006581biological_processacetylcholine catabolic process
A0007155biological_processcell adhesion
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017171molecular_functionserine hydrolase activity
A0031594cellular_componentneuromuscular junction
A0031623biological_processreceptor internalization
A0042166molecular_functionacetylcholine binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043236molecular_functionlaminin binding
A0045202cellular_componentsynapse
A0048471cellular_componentperinuclear region of cytoplasm
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
B0001919biological_processregulation of receptor recycling
B0002076biological_processosteoblast development
B0003990molecular_functionacetylcholinesterase activity
B0004104molecular_functioncholinesterase activity
B0005515molecular_functionprotein binding
B0005518molecular_functioncollagen binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0006581biological_processacetylcholine catabolic process
B0007155biological_processcell adhesion
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0017171molecular_functionserine hydrolase activity
B0031594cellular_componentneuromuscular junction
B0031623biological_processreceptor internalization
B0042166molecular_functionacetylcholine binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043236molecular_functionlaminin binding
B0045202cellular_componentsynapse
B0048471cellular_componentperinuclear region of cytoplasm
B0052689molecular_functioncarboxylic ester hydrolase activity
B0060041biological_processretina development in camera-type eye
B0095500biological_processacetylcholine receptor signaling pathway
B0098552cellular_componentside of membrane
B0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HI6 A 1543
ChainResidue
ATYR124
ATRP286
APHE297
ASER298
ATYR341
AHOH2249

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HI6 B 1543
ChainResidue
BSER298
BTYR341
BHOH2167
BTYR124
BTRP286
BPHE297

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CO3 A 1544
ChainResidue
ATRP286
AHIS287

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1KA A 1545
ChainResidue
ATYR382
AHIS393
AHOH2371

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1KA B 1544
ChainResidue
BASP304
BSER309
BASP310

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1KA A 1546
ChainResidue
AASP304
AGLY305
ASER309

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PE4 B 1545
ChainResidue
ALEU380
AHIS381
AGLN527
APHE535
BLEU380
BHIS381
BGLN527
BTHR528
BPHE535
B1KA1546
BHOH2206

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1KA B 1546
ChainResidue
AGLN527
BHIS381
BPE41545
BHOH2208
BHOH2269
BHOH2270

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1KA A 1547
ChainResidue
AGLU243
AARG246
AHOH2226
AHOH2378

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

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 Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASUN203
BSUN203

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AGLU334
AHIS447
BGLU334
BHIS447

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN265
BASN265

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN350
AASN464
BASN350
BASN464

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PDB entries from 2024-10-02

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