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1Q84

Crystal structure of the mouse acetylcholinesterase-TZ2PA6 anti complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004104molecular_functioncholinesterase activity
B0004104molecular_functioncholinesterase activity
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
DetailsActive site: {"description":"Acyl-ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
BGLU334
BHIS447
BSER203

246704

PDB entries from 2025-12-24

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