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6E67

Structure of beta2 adrenergic receptor fused to a Gs peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled 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
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
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
A0097746biological_processblood vessel diameter maintenance
B0003796molecular_functionlysozyme activity
B0004930molecular_functionG protein-coupled receptor activity
B0004941molecular_functionbeta2-adrenergic receptor activity
B0006940biological_processregulation of smooth muscle contraction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0009253biological_processpeptidoglycan catabolic process
B0016020cellular_componentmembrane
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
B0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue P0G A 3101
ChainResidue
ATRP109
AASN293
ATYR308
AILE309
AASN312
ATHR110
AASP113
AVAL114
APHE193
AALA200
ASER203
ASER204
ASER207

site_idAC2
Number of Residues11
Detailsbinding site for residue P0G B 3101
ChainResidue
BTRP109
BASP113
BVAL117
BPHE193
BALA200
BSER203
BSER207
BASN293
BTYR308
BILE309
BASN312

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues140
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AMET1-VAL34
ATHR96-CYS106
AARG175-ASN196
AGLN299-LYS305
BMET1-VAL34
BTHR96-CYS106
BARG175-ASN196
BGLN299-LYS305

site_idSWS_FT_FI2
Number of Residues46
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AGLY35-ILE58
BGLY35-ILE58

site_idSWS_FT_FI3
Number of Residues64
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AALA59-PHE71
AASP130-ALA150
BALA59-PHE71
BASP130-ALA150

site_idSWS_FT_FI4
Number of Residues46
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AILE72-LEU95
BILE72-LEU95

site_idSWS_FT_FI5
Number of Residues44
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLU107-VAL129
BGLU107-VAL129

site_idSWS_FT_FI6
Number of Residues46
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AARG151-TYR174
BARG151-TYR174

site_idSWS_FT_FI7
Number of Residues46
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLN197-SER220
BGLN197-SER220

site_idSWS_FT_FI8
Number of Residues46
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ALEU275-ILE298
BLEU275-ILE298

site_idSWS_FT_FI9
Number of Residues46
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AGLU306-SER329
BGLU306-SER329

site_idSWS_FT_FI10
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
AASP113
BTYR316
ATHR118
AASN293
AASN312
ATYR316
BASP113
BTHR118
BASN293
BASN312

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
ASER203
BSER203

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
ATYR141
BTYR141

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
ASER345
ASER346
BSER345
BSER346

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
ASER355
ASER356
BSER355
BSER356

site_idSWS_FT_FI15
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS341
BCYS341

site_idSWS_FT_FI16
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN6
AASN15
BASN6
BASN15

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PDB entries from 2024-09-18

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