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2R4R

Crystal structure of the human beta2 adrenoceptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004935molecular_functionadrenergic 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
A0016020cellular_componentmembrane
A0097746biological_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
AALA119-ILE135

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AMET1-VAL34
AMET96-CYS106
AARG175-ASN196
AGLN299-LYS305

site_idSWS_FT_FI2
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AGLY35-ILE58

site_idSWS_FT_FI3
Number of Residues85
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AALA59-PHE71
AASP130-ALA150
AARG221-THR274

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AILE72-LEU95

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLU107-VAL129

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AARG151-TYR174

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLN197-SER220

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ALEU275-ILE298

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AGLU306-SER329

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
AASP113
ATHR118
AASN293
AASN312
ATYR316

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
ASER203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
ATYR141

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ASER246

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
ASER261
ASER262

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
ASER345
ASER346

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
ASER355
ASER356

site_idSWS_FT_FI17
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS265

site_idSWS_FT_FI18
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS341

site_idSWS_FT_FI19
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN6
AASN15

218500

數據於2024-04-17公開中

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