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3UON

Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVmNLLIISFDRYFcV
ChainResidueDetails
AALA109-VAL125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues65
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AMET1-GLU22
ATHR81-ASP97
AGLN163-ALA184
ATHR411-PRO418

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AVAL23-MET45

site_idSWS_FT_FI3
Number of Residues55
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AVAL46-ASN59
AASP120-MET139
ACYS443-ARG466

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ATYR60-TYR80

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ALEU98-PHE119

site_idSWS_FT_FI6
Number of Residues22
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AALA140-TRP162

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AALA185-ILE209

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ATHR388-ASN410

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AASN419-LEU442

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000255
ChainResidueDetails
ATHR446
ATHR450
ATHR465

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASP2
AASP3
AASP6
AASP9

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

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PDB entries from 2024-10-30

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