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1CFJ

METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY REACTION WITH O-ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)

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
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019695biological_processcholine metabolic process
A0043083cellular_componentsynaptic cleft
A0045202cellular_componentsynapse
A0052689molecular_functioncarboxylic ester hydrolase activity
A0098552cellular_componentside of membrane
Functional Information from PDB Data
site_idCAT
Number of Residues3
DetailsCATALYTIC TRIAD
ChainResidue
ASER200
AHIS440
AGLU327

site_idOXY
Number of Residues3
DetailsCATALYTIC OXYANION HOLE
ChainResidue
AGLY118
AGLY119
AALA201

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
DetailsActive site: {"description":"Acyl-ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10368299","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16763558","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10368299","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16763558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1678899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10368299","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

238895

PDB entries from 2025-07-16

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