3dkk Summary

pdbe.org/3dkk
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Aged Form of Human Butyrylcholinesterase Inhibited by Tabun

The structure was published by Carletti, E., Li, H., Li, B., et al., Schopfer, L.M., Masson, P., and Nachon, F., in 2008 in a paper entitled "Aging of Cholinesterases Phosphylated by Tabun Proceeds through O-Dealkylation." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.31 Å and deposited in 2008.

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

The PDB entry contains the structure of Cholinesterase. This molecule has the UniProt identifier P06276 (CHLE_HUMAN)search. The sample contained 529 residues which is 92% of the natural sequence. Out of 529 residues 526 were observed and are deposited in the PDB.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Cholinesterase P06276 (29-557) (CHLE_HUMAN)search Homo sapienssearch 92% 529 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P06276 (29 - 557) Cholinesterase Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A (P06276) Rossmann foldsearch PF00135: Carboxylesterase familysearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P06276) beta-amyloid bindingsearch catalytic activitysearch acetylcholinesterase activitysearch cholinesterase activitysearch hydrolase activitysearch enzyme bindingsearch choline bindingsearch identical protein bindingsearch carboxylic ester hydrolase activitysearch extracellular regionsearch extracellular spacesearch nuclear envelope lumensearch endoplasmic reticulumsearch endoplasmic reticulum lumensearch membranesearch blood microparticlesearch response to nutrientsearch learningsearch negative regulation of cell proliferationsearch neuroblast differentiationsearch choline metabolic processsearch response to drugsearch response to alkaloidsearch cellular protein metabolic processsearch cocaine metabolic processsearch negative regulation of synaptic transmissionsearch response to glucocorticoidsearch response to folic acidsearch

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