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5D5B

In meso X-ray crystallography structure of the Beta2-adrenergic receptor at 100 K

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
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 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 Residues32
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AALA59-PHE71
AASP130-ALA150

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

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
ASER355
ASER356

site_idSWS_FT_FI15
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS265

site_idSWS_FT_FI16
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_FI17
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN6
AASN15

site_idSWS_FT_FI18
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI19
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI20
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI21
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

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PDB entries from 2024-11-06

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