Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6EMI

Crystal structure of a variant of human butyrylcholinesterase expressed in bacteria.

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	0050784	biological_process	cocaine catabolic 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
B	0001540	molecular_function	amyloid-beta binding
B	0003824	molecular_function	catalytic activity
B	0003990	molecular_function	acetylcholinesterase activity
B	0004104	molecular_function	cholinesterase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005641	cellular_component	nuclear envelope lumen
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005886	cellular_component	plasma membrane
B	0006581	biological_process	acetylcholine catabolic process
B	0006805	biological_process	xenobiotic metabolic process
B	0007584	biological_process	response to nutrient
B	0007612	biological_process	learning
B	0008285	biological_process	negative regulation of cell population proliferation
B	0009410	biological_process	response to xenobiotic stimulus
B	0014016	biological_process	neuroblast differentiation
B	0016486	biological_process	peptide hormone processing
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0019695	biological_process	choline metabolic process
B	0019899	molecular_function	enzyme binding
B	0033265	molecular_function	choline binding
B	0042802	molecular_function	identical protein binding
B	0043279	biological_process	response to alkaloid
B	0050784	biological_process	cocaine catabolic process
B	0050805	biological_process	negative regulation of synaptic transmission
B	0051384	biological_process	response to glucocorticoid
B	0051593	biological_process	response to folic acid
B	0052689	molecular_function	carboxylic ester hydrolase activity
B	0072562	cellular_component	blood microparticle

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue EDO A 601

Chain	Residue
A	ALA227
A	ALA229
A	VAL233
A	MET302
A	ASP304

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

Chain	Residue
A	LEU18
A	TRP98
A	ASP129
A	LYS131

site_id	AC3
Number of Residues	1
Details	binding site for residue EDO A 603

Chain	Residue
A	THR512

site_id	AC4
Number of Residues	7
Details	binding site for residue PEG A 604

Chain	Residue
A	ASN10
A	TYR33
A	PRO48
A	LEU49
A	TRP177
A	ASP180
A	ASN181

site_id	AC5
Number of Residues	1
Details	binding site for residue CL A 605

Chain	Residue
A	HOH740

site_id	AC6
Number of Residues	1
Details	binding site for residue CL A 606

Chain	Residue
A	ARG138

site_id	AC7
Number of Residues	2
Details	binding site for residue CL A 608

Chain	Residue
A	GLY30
A	LYS60

site_id	AC8
Number of Residues	1
Details	binding site for residue CL A 609

Chain	Residue
A	ARG254

site_id	AC9
Number of Residues	10
Details	binding site for residue PGE A 610

Chain	Residue
A	ASN159
A	GLU161
A	THR258
A	LYS314
A	THR315
A	GLN316
A	GLY413
A	ASN414
A	ASN415
A	HOH726

site_id	AD1
Number of Residues	6
Details	binding site for residue PGE A 611

Chain	Residue
A	GLY116
A	GLY117
A	SER198
A	TRP231
A	SER287
A	PHE329

site_id	AD2
Number of Residues	5
Details	binding site for residue PGE A 612

Chain	Residue
A	TRP82
A	GLY116
A	SER198
A	HIS438
A	HOH734

site_id	AD3
Number of Residues	2
Details	binding site for residue PGE A 613

Chain	Residue
A	SER53
A	ILE55

site_id	AD4
Number of Residues	7
Details	binding site for residue PGE A 614

Chain	Residue
A	TRP56
A	LYS60
A	TYR61
A	ALA62
A	ASN63
A	ASP87
A	TYR94

site_id	AD5
Number of Residues	3
Details	binding site for residue PGE A 615

Chain	Residue
A	GLU352
A	LYS355
A	GLU363

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO B 601

Chain	Residue
B	LEU18
B	TYR61
B	TRP98
B	ASP129
B	LYS131

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO B 602

Chain	Residue
B	TYR33
B	PRO48
B	LEU49
B	TRP177
B	ASP180

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO B 603

Chain	Residue
B	LYS60
B	ASN63
B	ASP87

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO B 604

Chain	Residue
B	HIS77
B	MET81
B	VAL127
B	EDO612

site_id	AE1
Number of Residues	4
Details	binding site for residue EDO B 605

Chain	Residue
B	LYS323
B	ASP324
B	GLU391
B	HOH830

site_id	AE2
Number of Residues	4
Details	binding site for residue EDO B 606

Chain	Residue
B	GLY115
B	GLY116
B	GLU197
B	EDO613

site_id	AE3
Number of Residues	2
Details	binding site for residue EDO B 607

Chain	Residue
B	TYR417
B	VAL492

site_id	AE4
Number of Residues	2
Details	binding site for residue EDO B 608

Chain	Residue
B	TRP56
B	HOH738

site_id	AE5
Number of Residues	3
Details	binding site for residue EDO B 609

Chain	Residue
B	ALA410
B	GLY413
B	ASN414

site_id	AE6
Number of Residues	2
Details	binding site for residue EDO B 610

Chain	Residue
B	ARG135
B	ARG465

site_id	AE7
Number of Residues	5
Details	binding site for residue EDO B 611

Chain	Residue
B	GLN172
B	GLY212
B	GLN484
B	PEG616
B	HOH705

site_id	AE8
Number of Residues	3
Details	binding site for residue EDO B 612

Chain	Residue
B	MET81
B	PRO126
B	EDO604

site_id	AE9
Number of Residues	6
Details	binding site for residue EDO B 613

Chain	Residue
B	SER198
B	PHE329
B	EDO606
B	PGE622
B	GLY116
B	GLY117

site_id	AF1
Number of Residues	3
Details	binding site for residue EDO B 614

Chain	Residue
B	HIS77
B	LYS427
B	PRO429

site_id	AF2
Number of Residues	10
Details	binding site for residue PEG B 615

Chain	Residue
B	GLY158
B	ASN159
B	THR218
B	ARG219
B	ASN256
B	GLU257
B	THR258
B	THR315
B	GLN316
B	HOH739

site_id	AF3
Number of Residues	9
Details	binding site for residue PEG B 616

Chain	Residue
B	LEU209
B	SER210
B	PRO211
B	GLY212
B	ASP297
B	PHE298
B	THR300
B	EDO611
B	HOH705

site_id	AF4
Number of Residues	3
Details	binding site for residue PEG B 617

Chain	Residue
B	ARG265
B	ASN266
B	LYS267

site_id	AF5
Number of Residues	1
Details	binding site for residue CL B 618

Chain	Residue
B	ASP387

site_id	AF6
Number of Residues	2
Details	binding site for residue CL B 619

Chain	Residue
B	ASN106
B	HOH874

site_id	AF7
Number of Residues	5
Details	binding site for residue PGE B 620

Chain	Residue
B	SER53
B	ILE55
B	TRP56
B	ASN57
B	PG4623

site_id	AF8
Number of Residues	7
Details	binding site for residue PGE B 621

Chain	Residue
B	HIS372
B	TYR373
B	THR374
B	ASP375
B	GLU391
B	ARG515
B	HIS518

site_id	AF9
Number of Residues	7
Details	binding site for residue PGE B 622

Chain	Residue
B	GLY116
B	GLY117
B	SER198
B	TRP231
B	LEU286
B	SER287
B	EDO613

site_id	AG1
Number of Residues	13
Details	binding site for residue PG4 B 623

Chain	Residue
B	LEU29
B	GLY30
B	TRP56
B	ASN57
B	ALA58
B	THR59
B	LYS60
B	ALA62
B	ASP91
B	TYR94
B	PGE620
B	HOH706
B	HOH738

site_id	AG2
Number of Residues	4
Details	binding site for residue PG4 B 624

Chain	Residue
B	ARG509
B	ILE510
B	MET511
B	THR512

Functional Information from PROSITE/UniProt

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

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

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22444575","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
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	4
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	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":"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	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":"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	2
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	4
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	2
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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)