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9OMT

X-ray structure of paraoxon (POX)-inhibited human acetylcholinesterase (hAChE) in complex with bis-oxime reactivator LG-1922

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG
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 Residues6
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4BDT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11053835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20408548","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B41","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X8B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EY8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

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