Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6IBL

ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST FORMOTEROL AND NANOBODY Nb80

Replaces:  6H7K
Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004935molecular_functionadrenergic receptor activity
A0004940molecular_functionbeta1-adrenergic receptor activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0016020cellular_componentmembrane
A0030337molecular_functionDNA polymerase processivity factor activity
A0045454biological_processcell redox homeostasis
A0045823biological_processpositive regulation of heart contraction
B0004930molecular_functionG protein-coupled receptor activity
B0004935molecular_functionadrenergic receptor activity
B0004940molecular_functionbeta1-adrenergic receptor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0007186biological_processG protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0015035molecular_functionprotein-disulfide reductase activity
B0015036molecular_functiondisulfide oxidoreductase activity
B0016020cellular_componentmembrane
B0030337molecular_functionDNA polymerase processivity factor activity
B0045454biological_processcell redox homeostasis
B0045823biological_processpositive regulation of heart contraction
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue H98 A 501
ChainResidue
AASP121
AASN310
AASN329
ATYR333
AVAL125
ACYS199
AASP200
APHE201
AALA208
ASER211
ASER215
APHE306

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 502
ChainResidue
ACYS192
AASP195
ACYS198
AHOH608

site_idAC3
Number of Residues12
Detailsbinding site for residue 2CV A 503
ChainResidue
ALEU171
ATRP181
AASN204
AALA206
ATYR207
AALA210
BVAL60
BILE63
BALA64
BGLY67
BSER68
BLEU92

site_idAC4
Number of Residues7
Detailsbinding site for residue 2CV A 504
ChainResidue
AGLU130
AARG157
AVAL160
ATHR164
BPHE97
BARG104
BTRP109

site_idAC5
Number of Residues6
Detailsbinding site for residue 2CV A 505
ChainResidue
ATHR81
ACYS85
ALEU120
ALYS159
AILE162
ACYS163

site_idAC6
Number of Residues5
Detailsbinding site for residue 2CV A 506
ChainResidue
ALEU220
ALEU289
ALYS290
ATHR300
ALEU304

site_idAC7
Number of Residues6
Detailsbinding site for residue 2CV A 507
ChainResidue
AALA206
AILE209
BILE63
BTHR81
BLEU93
B2CV504

site_idAC8
Number of Residues12
Detailsbinding site for residue H98 B 501
ChainResidue
BASP121
BVAL125
BCYS199
BASP200
BPHE201
BALA208
BSER211
BSER215
BPHE306
BASN310
BASN329
BTYR333

site_idAC9
Number of Residues5
Detailsbinding site for residue NA B 502
ChainResidue
BCYS192
BASP195
BCYS198
BHOH608
BHOH611

site_idAD1
Number of Residues2
Detailsbinding site for residue 2CV B 503
ChainResidue
BLEU289
BGLY293

site_idAD2
Number of Residues6
Detailsbinding site for residue 2CV B 504
ChainResidue
AARG205
A2CV507
BLEU78
BTHR81
BSER82
BLYS159

site_idAD3
Number of Residues1
Detailsbinding site for residue 2CV B 505
ChainResidue
BPHE174

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAIDRYLaI
ChainResidueDetails
AALA127-ILE143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER1032
ASER1035
BSER1032
BSER1035

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
AASP1026
BASP1026

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
AGLY1033
APRO1034
BGLY1033
BPRO1034

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS1069
BLYS1069

site_idSWS_FT_FI5
Number of Residues156
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18594507
ChainResidueDetails
ASER68-THR76
AASP138-ARG155
AARG232-ASN313
BSER68-THR76
BASP138-ARG155
BARG232-ASN313

site_idSWS_FT_FI6
Number of Residues52
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AASN77-VAL103
BASN77-VAL103

site_idSWS_FT_FI7
Number of Residues80
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18594507
ChainResidueDetails
AARG104-GLU115
AHIS180-ARG205
ACYS344-ASP348
BARG104-GLU115
BHIS180-ARG205
BCYS344-ASP348

site_idSWS_FT_FI8
Number of Residues42
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ALEU116-ILE137
BLEU116-ILE137

site_idSWS_FT_FI9
Number of Residues46
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AALA156-MET179
BALA156-MET179

site_idSWS_FT_FI10
Number of Residues50
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AALA206-TYR231
BALA206-TYR231

site_idSWS_FT_FI11
Number of Residues58
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AVAL314-TYR343
BVAL314-TYR343

site_idSWS_FT_FI12
Number of Residues44
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
APHE349-HIS371
BPHE349-HIS371

site_idSWS_FT_FI13
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4
ChainResidueDetails
AASP121
ASER211
ALEU357
BASP121
BSER211
BLEU357

site_idSWS_FT_FI14
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon