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5JQH

Structure of beta2 adrenoceptor bound to carazolol and inactive-state stabilizing nanobody, Nb60

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 Residues10
Detailsbinding site for residue CAU A 1401
ChainResidue
AASP1113
ATYR1316
AVAL1114
APHE1193
ASER1203
ASER1204
ATRP1286
APHE1289
APHE1290
AASN1312

site_idAC2
Number of Residues2
Detailsbinding site for residue CLR A 1402
ChainResidue
AILE1055
AVAL1081

site_idAC3
Number of Residues9
Detailsbinding site for residue CAU B 1401
ChainResidue
BASP1113
BVAL1114
BPHE1193
BSER1203
BPHE1289
BASN1293
BTYR1308
BASN1312
BTYR1316

site_idAC4
Number of Residues2
Detailsbinding site for residue CLR B 1402
ChainResidue
BILE1055
BVAL1081

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU876
BGLU876

site_idSWS_FT_FI2
Number of Residues2
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
AASP885
BASP885

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU897
APHE969
BLEU897
BPHE969

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER982
AASN997
BSER982
BASN997

site_idSWS_FT_FI5
Number of Residues46
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AGLY1035-ILE1058
BGLY1035-ILE1058

site_idSWS_FT_FI6
Number of Residues170
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AALA1059-PHE1071
AASP1130-ALA1150
AARG1221-ASP1300
BALA1059-PHE1071
BASP1130-ALA1150
BARG1221-ASP1300

site_idSWS_FT_FI7
Number of Residues46
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AILE1072-LEU1095
BILE1072-LEU1095

site_idSWS_FT_FI8
Number of Residues74
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ATHR1096-CYS1106
AARG1175-ASN1196
AILE1325-ASP1331
BTHR1096-CYS1106
BARG1175-ASN1196
BILE1325-ASP1331

site_idSWS_FT_FI9
Number of Residues44
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLU1107-VAL1129
BGLU1107-VAL1129

site_idSWS_FT_FI10
Number of Residues46
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AARG1151-TYR1174
BARG1151-TYR1174

site_idSWS_FT_FI11
Number of Residues46
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLN1197-SER1220
BGLN1197-SER1220

site_idSWS_FT_FI12
Number of Residues46
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AASN1301-LEU1324
BASN1301-LEU1324

site_idSWS_FT_FI13
Number of Residues46
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
AASP1113
BLEU1342
ATHR1118
ASER1319
AGLU1338
ALEU1342
BASP1113
BTHR1118
BSER1319
BGLU1338

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
ASER1203
BSER1203

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
ATYR1141
BTYR1141

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ALEU1272
BLEU1272

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
ALEU1287
APRO1288
BLEU1287
BPRO1288

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
AILE1291
BILE1291

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU876proton shuttle (general acid/base)
AASP885covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU876proton shuttle (general acid/base)
BASP885covalent catalysis

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PDB entries from 2024-07-17

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