9SCM
Crystal structure of Tc AChE with reactivator JDS364 Orthorhombic
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0003990 | molecular_function | acetylcholinesterase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006581 | biological_process | acetylcholine catabolic process |
| B | 0019695 | biological_process | choline metabolic process |
| B | 0043083 | cellular_component | synaptic cleft |
| B | 0045202 | cellular_component | synapse |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| D0Z0 | 0003990 | molecular_function | acetylcholinesterase activity |
| D0Z0 | 0005886 | cellular_component | plasma membrane |
| D0Z0 | 0006581 | biological_process | acetylcholine catabolic process |
| D0Z0 | 0019695 | biological_process | choline metabolic process |
| D0Z0 | 0043083 | cellular_component | synaptic cleft |
| D0Z0 | 0045202 | cellular_component | synapse |
| D0Z0 | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00122 |
| Number of Residues | 16 |
| Details | CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG |
| Chain | Residue | Details |
| D0Z0 | PHE187-GLY202 |
| site_id | PS00941 |
| Number of Residues | 11 |
| Details | CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP |
| Chain | Residue | Details |
| D0Z0 | GLU92-PRO102 |
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 | 4 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10368299","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16763558","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10368299","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
