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2CKM

Torpedo californica acetylcholinesterase complexed with alkylene- linked bis-tacrine dimer (7 carbon linker)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001507biological_processacetylcholine catabolic process in synaptic cleft
A0003990molecular_functionacetylcholinesterase activity
A0004104molecular_functioncholinesterase activity
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006581biological_processacetylcholine catabolic process
A0019695biological_processcholine metabolic process
A0043083cellular_componentsynaptic cleft
A0045202cellular_componentsynapse
A0052689molecular_functioncarboxylic ester hydrolase activity
A0098552cellular_componentside of membrane
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG
ChainResidueDetails
APHE187-GLY202

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP
ChainResidueDetails
AGLU92-PRO102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER200

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AGLU327
AHIS440

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:8597567
ChainResidueDetails
ASER543

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558
ChainResidueDetails
AASN59

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899
ChainResidueDetails
AASN416

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
ChainResidueDetails
AASN457
AASN533

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
ASER200
AHIS440
AGLU327

227561

PDB entries from 2024-11-20

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