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5F8U

Ligand occupancy in crystal structure of beta1-adrenergic receptor previously submitted by Huang et al

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004935molecular_functionadrenergic receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0004930molecular_functionG protein-coupled receptor activity
B0004935molecular_functionadrenergic receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue P32 B 400
ChainResidue
BTRP117
BPHE307
BASN310
BASN329
BTYR333
BTHR118
BASP121
BVAL122
BPHE201
BTHR203
BSER211
BTRP303
BPHE306

site_idAC2
Number of Residues15
Detailsbinding site for residue P32 A 400
ChainResidue
ATRP117
ATHR118
AASP121
AVAL122
APHE201
ATHR203
AALA208
ASER211
ASER212
ASER215
ATRP303
APHE306
APHE307
AASN310
AASN329

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAIDRYLaI
ChainResidueDetails
BALA127-ILE143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues68
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues68
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VT4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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