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6N48

Structure of beta2 adrenergic receptor bound to BI167107, Nanobody 6B9, and a positive allosteric modulator

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
A0016998biological_processcell wall macromolecule catabolic process
A0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue P0G A 1401
ChainResidue
ATRP1109
AASN1293
ATYR1308
AILE1309
AASN1312
ATYR1316
AASP1113
AVAL1114
ACYS1191
APHE1193
AALA1200
ASER1203
ASER1207
APHE1289

site_idAC2
Number of Residues3
Detailsbinding site for residue 1WV A 1402
ChainResidue
AMET1036
AMET1040
AILE1043

site_idAC3
Number of Residues8
Detailsbinding site for residue KBY A 1403
ChainResidue
AVAL1126
AASP1130
APHE1133
ASER1137
ALEU1144
ALEU1145
ALYS1149
AILE1153

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI
ChainResidueDetails
AALA1119-ILE1135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AGLY1035-ILE1058

site_idSWS_FT_FI2
Number of Residues85
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AALA1059-PHE1071
AASP1130-ALA1150
AARG1221-LEU1302

site_idSWS_FT_FI3
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AILE1072-LEU1095

site_idSWS_FT_FI4
Number of Residues37
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ATHR1096-CYS1106
AARG1175-ASN1196
AGLN1299-LYS1305

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLU1107-VAL1129

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AARG1151-TYR1174

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLN1197-SER1220

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ALEU1275-ILE1298

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AGLU1306-SER1329

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
AASP1113
ATHR1118
AASN1293
AASN1312
ATYR1316

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
ASER1203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
ATYR1141

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ATHR1274

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
APHE1289
APHE1290

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
ASER1345
ASER1346

site_idSWS_FT_FI16
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
AALA1265

site_idSWS_FT_FI17
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS1341

218853

数据于2024-04-24公开中

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