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8JJO

Cryo-EM structure of the beta2AR-mBRIL/1b3 Fab/Glue complex with an antagonist

Functional Information from GO Data
ChainGOidnamespacecontents
F0004930molecular_functionG protein-coupled receptor activity
F0004935molecular_functionadrenergic receptor activity
F0004941molecular_functionbeta2-adrenergic receptor activity
F0005506molecular_functioniron ion binding
F0006940biological_processregulation of smooth muscle contraction
F0007186biological_processG protein-coupled receptor signaling pathway
F0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
F0009055molecular_functionelectron transfer activity
F0016020cellular_componentmembrane
F0020037molecular_functionheme binding
F0022900biological_processelectron transport chain
F0042597cellular_componentperiplasmic space
F0097746biological_processblood vessel diameter maintenance
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI
ChainResidueDetails
FALA119-ILE135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
FGLY35-ILE58

site_idSWS_FT_FI2
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
FALA59-PHE71
FASP130-ALA150

site_idSWS_FT_FI3
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
FILE72-LEU95

site_idSWS_FT_FI4
Number of Residues37
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
FMET96-CYS106
FARG175-ASN196
FGLN366-LYS372

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
FGLU107-VAL129

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
FARG151-TYR174

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
FGLN197-SER220

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
FLEU342-ILE365

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
FGLU373-SER396

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
FASP113
FTHR118
FASN360
FASN379
FTYR383

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
FSER203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
FTYR141

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
FLEU329

site_idSWS_FT_FI14
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
FCYS332

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
FILE325
FTRP237

221051

PDB entries from 2024-06-12

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