Entry | Database: PDB / ID: 5fpq |
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Title | Structure of Homo sapiens acetylcholinesterase phosphonylated by sarin. |
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Components | ACETYLCHOLINESTERASE |
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Keywords | HYDROLASE / SIGNALING PROTEIN / ACETYLCHOLINESTERASE / SARIN / HI-6 / QM / DENSITY FUNCTIONAL THEORY CALCULATIONS / MICHAELIS COMPLEX. |
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Function / homology | Function and homology information
negative regulation of synaptic transmission, cholinergic / Neurotransmitter clearance / acetylcholine catabolic process in synaptic cleft / cholinesterase activity / serine hydrolase activity / acetylcholine catabolic process / acetylcholine binding / amyloid precursor protein metabolic process / acetylcholinesterase / acetylcholine receptor signaling pathway ...negative regulation of synaptic transmission, cholinergic / Neurotransmitter clearance / acetylcholine catabolic process in synaptic cleft / cholinesterase activity / serine hydrolase activity / acetylcholine catabolic process / acetylcholine binding / amyloid precursor protein metabolic process / acetylcholinesterase / acetylcholine receptor signaling pathway / osteoblast development / acetylcholinesterase activity / choline metabolic process / Synthesis of PC / basement membrane / regulation of receptor recycling / Synthesis, secretion, and deacylation of Ghrelin / side of membrane / synaptic cleft / laminin binding / synapse assembly / collagen binding / positive regulation of protein secretion / neuromuscular junction / receptor internalization / : / retina development in camera-type eye / nervous system development / positive regulation of cold-induced thermogenesis / amyloid-beta binding / hydrolase activity / cell adhesion / synapse / perinuclear region of cytoplasm / Golgi apparatus / cell surface / protein homodimerization activity / extracellular space / extracellular region / membrane / nucleus / plasma membraneSimilarity search - Function Acetylcholinesterase, tetramerisation domain / Acetylcholinesterase tetramerisation domain / Cholinesterase / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase type B, active site / Carboxylesterases type-B serine active site. / Carboxylesterase, type B / Carboxylesterase family / Alpha/Beta hydrolase fold, catalytic domain ...Acetylcholinesterase, tetramerisation domain / Acetylcholinesterase tetramerisation domain / Cholinesterase / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase type B, active site / Carboxylesterases type-B serine active site. / Carboxylesterase, type B / Carboxylesterase family / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha BetaSimilarity search - Domain/homology |
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Biological species | HOMO SAPIENS (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å |
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Authors | Allgardsson, A. / Berg, L. / Akfur, C. / Hornberg, A. / Worek, F. / Linusson, A. / Ekstrom, F. |
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2016 Title: Structure of a Prereaction Complex between the Nerve Agent Sarin, its Biological Target Acetylcholinesterase, and the Antidote Hi-6. Authors: Allgardsson, A. / Berg, L. / Akfur, C. / Hornberg, A. / Worek, F. / Linusson, A. / Ekstrom, F.J. |
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History | Deposition | Dec 2, 2015 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | May 11, 2016 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jun 1, 2016 | Group: Database references |
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Revision 2.0 | Jan 17, 2018 | Group: Atomic model / Data collection / Category: atom_site / diffrn_source Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.label_atom_id / _diffrn_source.pdbx_synchrotron_site |
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Revision 2.1 | Jan 10, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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