6O4W

Binary complex of native hAChE with Donepezil

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001507	biological_process	acetylcholine catabolic process in synaptic cleft
A	0001540	molecular_function	amyloid-beta binding
A	0002076	biological_process	osteoblast development
A	0003990	molecular_function	acetylcholinesterase activity
A	0004104	molecular_function	cholinesterase activity
A	0005515	molecular_function	protein binding
A	0005518	molecular_function	collagen binding
A	0005576	cellular_component	extracellular region
A	0005604	cellular_component	basement membrane
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005794	cellular_component	Golgi apparatus
A	0005886	cellular_component	plasma membrane
A	0006581	biological_process	acetylcholine catabolic process
A	0007155	biological_process	cell adhesion
A	0007399	biological_process	nervous system development
A	0007416	biological_process	synapse assembly
A	0009986	cellular_component	cell surface
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0017171	molecular_function	serine hydrolase activity
A	0031594	cellular_component	neuromuscular junction
A	0032223	biological_process	negative regulation of synaptic transmission, cholinergic
A	0042166	molecular_function	acetylcholine binding
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042982	biological_process	amyloid precursor protein metabolic process
A	0043083	cellular_component	synaptic cleft
A	0043236	molecular_function	laminin binding
A	0045202	cellular_component	synapse
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050714	biological_process	positive regulation of protein secretion
A	0052689	molecular_function	carboxylic ester hydrolase activity
A	0098552	cellular_component	side of membrane
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	0001507	biological_process	acetylcholine catabolic process in synaptic cleft
B	0001540	molecular_function	amyloid-beta binding
B	0002076	biological_process	osteoblast development
B	0003990	molecular_function	acetylcholinesterase activity
B	0004104	molecular_function	cholinesterase activity
B	0005515	molecular_function	protein binding
B	0005518	molecular_function	collagen binding
B	0005576	cellular_component	extracellular region
B	0005604	cellular_component	basement membrane
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005794	cellular_component	Golgi apparatus
B	0005886	cellular_component	plasma membrane
B	0006581	biological_process	acetylcholine catabolic process
B	0007155	biological_process	cell adhesion
B	0007399	biological_process	nervous system development
B	0007416	biological_process	synapse assembly
B	0009986	cellular_component	cell surface
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0017171	molecular_function	serine hydrolase activity
B	0031594	cellular_component	neuromuscular junction
B	0032223	biological_process	negative regulation of synaptic transmission, cholinergic
B	0042166	molecular_function	acetylcholine binding
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0042982	biological_process	amyloid precursor protein metabolic process
B	0043083	cellular_component	synaptic cleft
B	0043236	molecular_function	laminin binding
B	0045202	cellular_component	synapse
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050714	biological_process	positive regulation of protein secretion
B	0052689	molecular_function	carboxylic ester hydrolase activity
B	0098552	cellular_component	side of membrane
B	0120162	biological_process	positive regulation of cold-induced thermogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue GOL A 601

Chain	Residue
A	GLU81
A	MET85
A	THR436
A	LEU437
A	SER438
A	TYR449
A	GLU452
A	HOH842

---

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL A 602

Chain	Residue
A	E20604
A	HOH718
A	HOH788
A	TYR341

---

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 603

Chain	Residue
A	ARG46
A	ARG274
A	THR275
A	PRO277
A	HOH833

---

site_id	AC4
Number of Residues	13
Details	binding site for residue E20 A 604

Chain	Residue
A	TYR72
A	TRP86
A	TYR124
A	GLU202
A	TRP286
A	SER293
A	PHE295
A	TYR337
A	PHE338
A	TYR341
A	GOL602
A	HOH708
A	HOH832

---

site_id	AC5
Number of Residues	3
Details	binding site for residue NO3 A 605

Chain	Residue
A	ASP333
A	TRP442
A	HOH755

---

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL B 601

Chain	Residue
B	GLU81
B	MET85
B	THR436
B	LEU437
B	SER438
B	TYR449
B	GLU452
B	HOH846

---

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL B 602

Chain	Residue
B	LEU76
B	TYR341
B	E20604
B	HOH712
B	HOH789
B	HOH811

---

site_id	AC8
Number of Residues	3
Details	binding site for residue GOL B 603

Chain	Residue
B	ARG274
B	PRO277
B	HOH755

---

site_id	AC9
Number of Residues	13
Details	binding site for residue E20 B 604

Chain	Residue
B	TYR72
B	TRP86
B	TYR124
B	GLU202
B	TRP286
B	SER293
B	PHE295
B	TYR337
B	PHE338
B	TYR341
B	GOL602
B	HOH701
B	HOH847

---

site_id	AD1
Number of Residues	4
Details	binding site for residue NO3 B 605

Chain	Residue
B	LYS332
B	ASP333
B	GLU396
B	TRP442

---

site_id	AD2
Number of Residues	2
Details	binding site for residue NO3 B 606

Chain	Residue
B	PRO36
B	TYR98

---

site_id	AD3
Number of Residues	4
Details	binding site for residue NO3 B 607

Chain	Residue
B	PRO88
B	ASN89
B	ARG90
B	GLU91

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE190-GLY205

---

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

Chain	Residue	Details
A	GLU94-PRO104

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Acyl-ester intermediate"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PDB","id":"4BDT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11053835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20408548","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B41","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1F8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X8B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EY8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23035744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EY8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---