Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DAJ

Structure of the M3 Muscarinic Acetylcholine Receptor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0003796	molecular_function	lysozyme activity
B	0003824	molecular_function	catalytic activity
B	0004930	molecular_function	G protein-coupled receptor activity
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0009253	biological_process	peptidoglycan catabolic process
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0030430	cellular_component	host cell cytoplasm
B	0031640	biological_process	killing of cells of another organism
B	0042742	biological_process	defense response to bacterium
B	0044659	biological_process	viral release from host cell by cytolysis
C	0003796	molecular_function	lysozyme activity
C	0003824	molecular_function	catalytic activity
C	0004930	molecular_function	G protein-coupled receptor activity
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0009253	biological_process	peptidoglycan catabolic process
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016998	biological_process	cell wall macromolecule catabolic process
C	0030430	cellular_component	host cell cytoplasm
C	0031640	biological_process	killing of cells of another organism
C	0042742	biological_process	defense response to bacterium
C	0044659	biological_process	viral release from host cell by cytolysis
D	0003796	molecular_function	lysozyme activity
D	0003824	molecular_function	catalytic activity
D	0004930	molecular_function	G protein-coupled receptor activity
D	0007186	biological_process	G protein-coupled receptor signaling pathway
D	0009253	biological_process	peptidoglycan catabolic process
D	0016020	cellular_component	membrane
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016998	biological_process	cell wall macromolecule catabolic process
D	0030430	cellular_component	host cell cytoplasm
D	0031640	biological_process	killing of cells of another organism
D	0042742	biological_process	defense response to bacterium
D	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 0HK A 2000

Chain	Residue
A	ASP147
A	ASN507
A	TYR529
A	CYS532
A	TYR148
A	SER151
A	ASN152
A	TRP199
A	ALA238
A	PHE239
A	TRP503
A	TYR506

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 2001

Chain	Residue
A	ASN1144
A	ARG1148
D	ARG1080

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 2002

Chain	Residue
A	ARG1014
A	LEU1015
A	LYS1016
D	LYS1083

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 2003

Chain	Residue
A	ASN1116
D	LYS178
D	LYS1060

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 2004

Chain	Residue
A	LYS178
A	LYS1060
D	ASN1116

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 0HK B 2000

Chain	Residue
B	ASP147
B	TYR148
B	SER151
B	ASN152
B	TRP199
B	THR231
B	THR234
B	ALA238
B	PHE239
B	TRP503
B	TYR506
B	ASN507
B	TYR529
B	CYS532

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 2001

Chain	Residue
B	LYS178
B	LYS1060

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 0HK C 2000

Chain	Residue
C	ASP147
C	TYR148
C	SER151
C	ASN152
C	TRP199
C	THR231
C	THR234
C	ALA235
C	ALA238
C	PHE239
C	TRP503
C	TYR506
C	ASN507
C	TYR529
C	CYS532

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 C 2001

Chain	Residue
C	LYS178
C	LYS1060

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 C 2002

Chain	Residue
C	ARG1119

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 0HK D 2000

Chain	Residue
D	ASP147
D	TYR148
D	SER151
D	ASN152
D	TRP199
D	PHE239
D	TRP503
D	TYR506
D	ASN507
D	TYR529
D	CYS532

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 D 2001

Chain	Residue
A	ARG1137
D	ARG176

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 D 2002

Chain	Residue
A	ARG176
D	ARG1137

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 2003

Chain	Residue
A	LYS1083
D	ARG1014
D	LEU1015
D	LYS1016

Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVmNLLVISFDRYFsI

Chain	Residue	Details
A	ALA153-ILE169

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	92
Details	Transmembrane: {"description":"Helical; Name=1"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	124
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"22358844","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=2"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	176
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"22358844","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=3"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=4"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=5"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=6"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Name=7"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9ERZ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASP1020	covalent catalysis

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
B	GLU1011	proton shuttle (general acid/base)
B	ASP1020	covalent catalysis

site_id	MCSA3
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
C	GLU1011	proton shuttle (general acid/base)
C	ASP1020	covalent catalysis

site_id	MCSA4
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
D	GLU1011	proton shuttle (general acid/base)
D	ASP1020	covalent catalysis

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