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7BVQ

Structure of human beta1 adrenergic receptor bound to carazolol

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
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0004930molecular_functionG protein-coupled receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0009253biological_processpeptidoglycan catabolic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0030430cellular_componenthost cell cytoplasm
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044659biological_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. ASIeTLCVIALDRYLaI
ChainResidueDetails
AALA1144-ILE1160

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250
ChainResidueDetails
AGLN1056-ALA1084
BGLN1056-ALA1084

site_idSWS_FT_FI2
Number of Residues190
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
ALYS1085-THR1093
AASP1155-ARG1172
AARG1249-ASN1373
BLYS1085-THR1093
BASP1155-ARG1172
BARG1249-ASN1373

site_idSWS_FT_FI3
Number of Residues52
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250
ChainResidueDetails
AASN1094-VAL1120
BASN1094-VAL1120

site_idSWS_FT_FI4
Number of Residues80
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
ATRP1121-GLU1132
AHIS1197-ARG1222
BTRP1121-GLU1132
BHIS1197-ARG1222

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250
ChainResidueDetails
ALEU1133-LEU1154
BLEU1133-LEU1154

site_idSWS_FT_FI6
Number of Residues46
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
AALA1173-MET1196
BALA1173-MET1196

site_idSWS_FT_FI7
Number of Residues50
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
AALA1223-PHE1248
BALA1223-PHE1248

site_idSWS_FT_FI8
Number of Residues58
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues44
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
AGLY1366
BGLY1366

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails

237735

PDB entries from 2025-06-18

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