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6N48

Structure of beta2 adrenergic receptor bound to BI167107, Nanobody 6B9, and a positive allosteric modulator

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0004941molecular_functionbeta2-adrenergic receptor activity
A0006940biological_processregulation of smooth muscle contraction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
A0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue P0G A 1401
ChainResidue
ATRP1109
AASN1293
ATYR1308
AILE1309
AASN1312
ATYR1316
AASP1113
AVAL1114
ACYS1191
APHE1193
AALA1200
ASER1203
ASER1207
APHE1289

site_idAC2
Number of Residues3
Detailsbinding site for residue 1WV A 1402
ChainResidue
AMET1036
AMET1040
AILE1043

site_idAC3
Number of Residues8
Detailsbinding site for residue KBY A 1403
ChainResidue
AVAL1126
AASP1130
APHE1133
ASER1137
ALEU1144
ALEU1145
ALYS1149
AILE1153

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI
ChainResidueDetails
AALA1119-ILE1135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues37
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2540197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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