7P1P
Crystal structure of human acetylcholinesterase in complex with (E)-3-hydroxy-6-(3-(4-(4-(((2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)butyl)-1H-1,2,3-triazol-1-yl)propyl)picolinaldehyde oxime
This is a non-PDB format compatible entry.
Functional Information from GO Data
Functional Information from PROSITE/UniProt
| site_id | PS00122 |
| Number of Residues | 16 |
| Details | CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG |
| Chain | Residue | Details |
| aa | PHE190-GLY205 |
| site_id | PS00941 |
| Number of Residues | 11 |
| Details | CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP |
| Chain | Residue | Details |
| aa | GLU94-PRO104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4BDT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EY8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
