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1p0i Summary pdbe.org/1p0i
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PDB entry 1p0i

Crystal structure of human butyryl cholinesterase

The structure was published by Nicolet, Y., Lockridge, O., Masson, P., Fontecilla-Camps, J.C., and Nachon, F., in 2003 in a paper entitled "Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2003.

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 522 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 98%

This entry contains 1 unique UniProt protein:

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

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P06276) Acetylcholinesterase-likesearch Rossmann foldsearch Carboxylesterasesearch, Acetylcholinesterase tetramerisation domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P06276) Beta-amyloid bindingsearch, Catalytic activitysearch, Acetylcholinesterase activitysearch, Carboxylesterase activitysearch, Cholinesterase activitysearch, Hydrolase activitysearch, Enzyme bindingsearch, Choline bindingsearch Extracellular regionsearch, Extracellular spacesearch, Membrane fractionsearch, Nuclear envelope lumensearch, Endoplasmic reticulumsearch, Endoplasmic reticulum lumensearch Synaptic transmission, cholinergicsearch, Response to nutrientsearch, Learningsearch, Metabolic processsearch, Choline metabolic processsearch, Response to drugsearch, Response to alkaloidsearch, Cocaine metabolic processsearch, Negative regulation of synaptic transmissionsearch, Response to glucocorticoid stimulussearch, Response to folic acidsearch

Chain InterPro annotation
A Cholinesterasesearch, Carboxylesterase, type Bsearch, Acetylcholinesterase, tetramerisationsearch, Carboxylesterase type B, conserved sitesearch, Carboxylesterase type B, active sitesearch