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4U14

Structure of the M3 muscarinic acetylcholine receptor bound to the antagonist tiotropium crystallized with disulfide-stabilized T4 lysozyme (dsT4L)

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 PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 0HK A 2000
ChainResidue
AASP147
ATYR529
ACYS532
ATYR148
ASER151
ATRP199
ALEU225
ATHR231
ATRP503
ATYR506
AASN507

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVmNLLVISFDRYFsI
ChainResidueDetails
AALA153-ILE169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AVAL67-VAL90

site_idSWS_FT_FI2
Number of Residues31
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22358844
ChainResidueDetails
AALA91-ASN103
AASP164-ARG183

site_idSWS_FT_FI3
Number of Residues25
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ATYR104-ILE129

site_idSWS_FT_FI4
Number of Residues44
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:22358844
ChainResidueDetails
AMET130-ASP141
ATRP206-PRO228
ATHR514-TRP525

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ALEU142-PHE163

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AALA184-PHE205

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
ATHR229-TRP251

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ATHR491-ASN513

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AASN526-LEU545

site_idSWS_FT_FI10
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_FI11
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_FI12
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI13
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 2024-07-24

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