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6OL9

Structure of the M5 muscarinic acetylcholine receptor (M5-T4L) bound to tiotropium

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
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 Residues1
Detailsbinding site for residue OLA A 1201
ChainResidue
AVAL490

site_idAC2
Number of Residues8
Detailsbinding site for residue OLA A 1202
ChainResidue
AASN115
AMET119
APRO164
AALA165
ACYS168
ATRP169
ALEU172
AALA200

site_idAC3
Number of Residues14
Detailsbinding site for residue 0HK A 1203
ChainResidue
AASP110
ATYR111
ASER114
AASN115
ATHR194
ATHR197
AALA198
APHE202
ATRP455
ATYR458
AASN459
ATYR481
ACYS484
ATYR485

site_idAC4
Number of Residues9
Detailsbinding site for residue P33 A 1204
ChainResidue
ATYR87
ATYR111
ACYS183
AGLN184
AILE185
ALEU188
ASER189
ATRP477
AHIS478

site_idAC5
Number of Residues8
Detailsbinding site for residue OLC A 1205
ChainResidue
ALYS62
ATYR67
APRO144
ALYS145
AGLY148
APHE159
ACYS471
ALEU476

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues31
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues50
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues9
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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