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5F8U

Ligand occupancy in crystal structure of beta1-adrenergic receptor previously submitted by Huang et al

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004935molecular_functionadrenergic receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0004930molecular_functionG protein-coupled receptor activity
B0004935molecular_functionadrenergic receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue P32 B 400
ChainResidue
BTRP117
BPHE307
BASN310
BASN329
BTYR333
BTHR118
BASP121
BVAL122
BPHE201
BTHR203
BSER211
BTRP303
BPHE306

site_idAC2
Number of Residues15
Detailsbinding site for residue P32 A 400
ChainResidue
ATRP117
ATHR118
AASP121
AVAL122
APHE201
ATHR203
AALA208
ASER211
ASER212
ASER215
ATRP303
APHE306
APHE307
AASN310
AASN329

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAIDRYLaI
ChainResidueDetails
BALA127-ILE143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
BGLN39-GLY67
AGLN39-GLY67

site_idSWS_FT_FI2
Number of Residues156
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18594507
ChainResidueDetails
BSER68-THR76
BASP138-ARG155
BARG232-PHE315
ASER68-THR76
AASP138-ARG155
AARG232-PHE315

site_idSWS_FT_FI3
Number of Residues52
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
BASN77-VAL103
AASN77-VAL103

site_idSWS_FT_FI4
Number of Residues80
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18594507
ChainResidueDetails
BARG104-GLU115
BHIS180-ARG205
BSER346-ARG350
AARG104-GLU115
AHIS180-ARG205
ASER346-ARG350

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
BLEU116-ILE137
ALEU116-ILE137

site_idSWS_FT_FI6
Number of Residues46
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
BALA156-MET179
AALA156-MET179

site_idSWS_FT_FI7
Number of Residues50
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
BALA206-TYR231
AALA206-TYR231

site_idSWS_FT_FI8
Number of Residues58
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
BASN316-ARG345
AASN316-ARG345

site_idSWS_FT_FI9
Number of Residues44
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
BLYS351-HIS373
ALYS351-HIS373

site_idSWS_FT_FI10
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4
ChainResidueDetails
BASP121
BSER211
BPHE359
AASP121
ASER211
APHE359

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails

224004

PDB entries from 2024-08-21

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