3lii Summary

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Recombinant human acetylcholinesterase

The structure was published by Dvir, H., Silman, I., Harel, M., Rosenberry, T.L., and Sussman, J.L., in 2010 in a paper entitled "Acetylcholinesterase: From 3D structure to function." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.2 Å and deposited in 2010.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Acetylcholinesterase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Acetylcholinesterase P22303 (35-574) (ACES_HUMAN)search Homo sapienssearch 92% 540 98%
B Acetylcholinesterase P22303 (35-574) (ACES_HUMAN)search Homo sapienssearch 92% 540 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P22303 (35 - 574) Acetylcholinesterase Homo sapiens

Chain Sequence family (Pfam)
A, B (P22303) PF00135: Carboxylesterase familysearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A, B (P22303) positive regulation of protein secretionsearch regulation of axonogenesissearch phospholipid metabolic processsearch protein tetramerizationsearch choline metabolic processsearch response to woundingsearch osteoblast developmentsearch cell adhesionsearch synapse assemblysearch synaptic transmission, cholinergicsearch nervous system developmentsearch amyloid precursor protein metabolic processsearch retina development in camera-type eyesearch glycerophospholipid biosynthetic processsearch acetylcholine catabolic process in synaptic cleftsearch acetylcholine catabolic processsearch regulation of dendrite morphogenesissearch cell proliferationsearch synaptic transmissionsearch receptor internalizationsearch negative regulation of synaptic transmission, cholinergicsearch muscle organ developmentsearch phosphatidylcholine biosynthetic processsearch DNA replicationsearch regulation of receptor recyclingsearch neurotransmitter biosynthetic processsearch small molecule metabolic processsearch neurotransmitter catabolic processsearch neurotransmitter receptor biosynthetic processsearch cell junctionsearch anchored component of membranesearch cell surfacesearch synapsesearch extracellular spacesearch plasma membranesearch extracellular regionsearch neuromuscular junctionsearch axonsearch membranesearch presynaptic membranesearch postsynaptic membranesearch perinuclear region of cytoplasmsearch nucleussearch endoplasmic reticulum lumensearch basal laminasearch Golgi apparatussearch dendritesearch acetylcholinesterase activitysearch carboxylic ester hydrolase activitysearch cholinesterase activitysearch acetylcholine bindingsearch laminin bindingsearch protein homodimerization activitysearch protein bindingsearch serine hydrolase activitysearch hydrolase activitysearch protein self-associationsearch beta-amyloid bindingsearch collagen bindingsearch

Chain InterPro annotation
A, B Cholinesterasesearch Carboxylesterase, type Bsearch Acetylcholinesterase, tetramerisation domainsearch Carboxylesterase type B, conserved sitesearch Carboxylesterase type B, active sitesearch Alpha/Beta hydrolase foldsearch