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2YCW

TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CARAZOLOL

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 Residues11
DetailsBINDING SITE FOR RESIDUE CAU A 400
ChainResidue
ATRP117
AASN329
ATYR333
AASP121
AVAL122
APHE201
ATYR207
ASER211
ASER215
APHE306
AASN310

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CAU B 400
ChainResidue
BTRP117
BASP121
BPHE201
BTYR207
BSER211
BPHE306
BPHE307
BASN310
BASN329
BTYR333

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 2CV A 1360
ChainResidue
AHIS286
ALEU289
ALYS290
AMET296

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 2CV A 1361
ChainResidue
APRO176
ATRP181
AGLU185
AASN204
AARG205
AALA206
BVAL160
B2CV1362

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 2CV B 1360
ChainResidue
AVAL160
ATHR164
BTRP181
BALA206

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 2CV B 1362
ChainResidue
A2CV1361
BARG157
BVAL160

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 1362
ChainResidue
ASER111
AASP195
ACYS198

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 1363
ChainResidue
BSER111
BCYS192
BASP195
BCYS198

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 Residues56
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues80
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues58
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VT4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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