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6MXT

Crystal structure of human beta2 adrenergic receptor bound to salmeterol and Nb71

Replaces:  6CSY
Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic 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
A0008152biological_processmetabolic process
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
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 PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue K5Y A 1401
ChainResidue
AASP1113
ASER1207
APHE1289
AASN1293
AHIS1296
AILE1303
ATYR1308
AILE1309
AASN1312
ATYR1316
AVAL1114
AVAL1117
ACYS1191
AASP1192
APHE1193
APHE1194
ATYR1199
ASER1203

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 1402
ChainResidue
AASN1103
ACYS1184
ATYR1185
AGLU1187
ACYS1190
AHOH1517

site_idAC3
Number of Residues3
Detailsbinding site for residue NI A 1403
ChainResidue
AGLU1107
AHIS1172
AHOH1516

site_idAC4
Number of Residues2
Detailsbinding site for residue OLC A 1404
ChainResidue
AHIS1269
ALEU1272

site_idAC5
Number of Residues7
Detailsbinding site for residue HTO A 1405
ChainResidue
AGLU10
AASP19
AGLU21
ATHR25
AGLY29
AGLN104
AARG144

site_idAC6
Number of Residues3
Detailsbinding site for residue OLA A 1406
ChainResidue
ALEU1163
ATHR1164
AALA1198

site_idAC7
Number of Residues3
Detailsbinding site for residue P33 A 1407
ChainResidue
ALEU32
ALYS34
AGLN104

site_idAC8
Number of Residues5
Detailsbinding site for residue NI N 201
ChainResidue
AASP1234
AHIS1269
AHOH1505
NHIS119
NHIS121

site_idAC9
Number of Residues3
Detailsbinding site for residue NI N 202
ChainResidue
NHIS117
NHIS120
NHIS122

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 Residues2
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
ASER1355
ASER1356

site_idSWS_FT_FI17
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
AYCM1265

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
AYCM1341

site_idSWS_FT_FI19
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
AGLU10

site_idSWS_FT_FI20
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
AASP19

site_idSWS_FT_FI21
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU31
APHE103

site_idSWS_FT_FI22
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER116
AASN131

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU10proton shuttle (general acid/base)
AASP19covalent catalysis

218853

PDB entries from 2024-04-24

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