Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1QIE

SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME POINTS (POINT B) CAUSED BY INTENSE SYNCHROTRON RADIATION TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE

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
AGLU327
AHIS440

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

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon