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8GGW

Locally refined cryoEM structure of receptor from beta-2-adrenergic receptor in complex with GTP-bound Gs heterotrimer (transition intermediate #15 of 20)

Functional Information from GO Data
ChainGOidnamespacecontents
R0004930molecular_functionG protein-coupled receptor activity
R0004935molecular_functionadrenergic receptor activity
R0004941molecular_functionbeta2-adrenergic receptor activity
R0006940biological_processregulation of smooth muscle contraction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0097746biological_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
RALA119-ILE135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
RMET-6-GLN27
RTHR96-CYS106
RARG175-ASN196
RGLN299-LYS305

site_idSWS_FT_FI2
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
RGLY35-ILE58

site_idSWS_FT_FI3
Number of Residues168
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
RALA59-PHE71
RASP130-ALA150
RARG221-THR274
RPRO323-ASN406

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
RILE72-LEU95

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
RGLU107-VAL129

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
RARG151-TYR174

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
RGLN197-SER220

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
RLEU275-ILE298

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
RGLU306-SER329

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
RASP113
RTHR118
RASN293
RASN312
RTYR316

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
RSER203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
RTYR141

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
RSER246

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
RSER261
RSER262

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
RSER345
RSER346

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
RSER355
RSER356

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:19584355
ChainResidueDetails
RPRO390
RPRO403

site_idSWS_FT_FI18
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
RCYS265

site_idSWS_FT_FI19
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
RCYS341

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
RASN-1
RASN8

227111

PDB entries from 2024-11-06

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