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7AIT

Crystal structure of Torpedo Californica acetylcholinesterase in complex with 7-[(3-Chloro-6,7,10,11-tetrahydro-9-methyl-7,11-methanocycloocta[b]quinolin-12-yl)amino]-N-(4-hydroxy-3-methoxybenzyl)heptanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0001507biological_processacetylcholine catabolic process in synaptic cleft
A0003990molecular_functionacetylcholinesterase activity
A0004104molecular_functioncholinesterase activity
B0001507biological_processacetylcholine catabolic process in synaptic cleft
B0003990molecular_functionacetylcholinesterase activity
B0004104molecular_functioncholinesterase activity
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 Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER200
BSER200

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AGLU327
AHIS440
BGLU327
BHIS440

site_idSWS_FT_FI3
Number of Residues2
DetailsLIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:8597567
ChainResidueDetails
ASER543
BSER543

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558
ChainResidueDetails
AASN59
BASN59

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899
ChainResidueDetails
AASN416
BASN416

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299
ChainResidueDetails
AASN457
AASN533
BASN457
BASN533

226707

PDB entries from 2024-10-30

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