1XLU

X-Ray Structure Of Di-Isopropyl-Phosphoro-Fluoridate (Dfp) Inhibited Butyrylcholinesterase after Aging

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001540	molecular_function	amyloid-beta binding
A	0003824	molecular_function	catalytic activity
A	0003990	molecular_function	acetylcholinesterase activity
A	0004104	molecular_function	cholinesterase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005641	cellular_component	nuclear envelope lumen
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005886	cellular_component	plasma membrane
A	0006581	biological_process	acetylcholine catabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0007584	biological_process	response to nutrient
A	0007612	biological_process	learning
A	0008285	biological_process	negative regulation of cell population proliferation
A	0009410	biological_process	response to xenobiotic stimulus
A	0014016	biological_process	neuroblast differentiation
A	0016486	biological_process	peptide hormone processing
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0019695	biological_process	choline metabolic process
A	0019899	molecular_function	enzyme binding
A	0033265	molecular_function	choline binding
A	0042802	molecular_function	identical protein binding
A	0043279	biological_process	response to alkaloid
A	0050783	biological_process	cocaine metabolic process
A	0050805	biological_process	negative regulation of synaptic transmission
A	0051384	biological_process	response to glucocorticoid
A	0051593	biological_process	response to folic acid
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	0072562	cellular_component	blood microparticle

Functional Information from PROSITE/UniProt

site_id	PS00122
Number of Residues	16
Details	CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpksVtLfGeSAG

Chain	Residue	Details
A	PHE185-GLY200

---

site_id	PS00941
Number of Residues	11
Details	CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWiP

Chain	Residue	Details
A	GLU90-PRO100

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"4BDS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22444575","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17768338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17768338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3542989","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17768338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1qe3

Chain	Residue	Details
A	GLU325
A	HIS438
A	SER198

---