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2Y01

TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB102)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004935molecular_functionadrenergic receptor activity
A0004940molecular_functionbeta1-adrenergic receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0045823biological_processpositive regulation of heart contraction
B0004930molecular_functionG protein-coupled receptor activity
B0004935molecular_functionadrenergic receptor activity
B0004940molecular_functionbeta1-adrenergic receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
B0045823biological_processpositive regulation of heart contraction
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE Y01 A 401
ChainResidue
AARG157
AILE161
AHOH2019
BARG205
BALA206
B2CV501

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE Y01 A 402
ChainResidue
AGLY67
ALEU78
ATRP166

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 2CV A 501
ChainResidue
AHIS180
ATRP181
AARG183
AASP184
AASN204
AHOH2020
BVAL160
BTHR164
BY01401
B2CV505

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE 2CV A 502
ChainResidue
ALEU289

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 2CV A 503
ChainResidue
AARG205
AVAL314
APHE315
BLEU152
BARG157
BY01401

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 2CV A 504
ChainResidue
AVAL51
AVAL326
AMET338
AY00601

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 2CV A 505
ChainResidue
ALYS159
AVAL160
ACYS163
BGLU185
B2CV501

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE Y00 A 601
ChainResidue
AASP121
ASER211
APHE306
APHE307
AASN310
AASN329
ATRP330
ATYR333
A2CV504

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE Y01 B 401
ChainResidue
AALA206
A2CV501
A2CV503
AHOH2020
BCYS133
BARG157
BVAL160
BILE214

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE Y01 B 402
ChainResidue
BLEU78
BLYS159
BTRP166

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 2CV B 501
ChainResidue
AVAL160
ATHR164
AY01401
A2CV505
BPRO176
BTRP181
BASP184
BGLU185

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 2CV B 502
ChainResidue
BTYR231
BHIS286
BLEU289
BGLY293

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 2CV B 503
ChainResidue
AARG157
BPHE315

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 2CV B 504
ChainResidue
BMET48
BTRP330

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 2CV B 505
ChainResidue
AGLU185
A2CV501
BLYS159
BVAL160
BCYS163
BTRP166

site_idBC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE Y00 B 601
ChainResidue
BVAL102
BTRP117
BTHR118
BASP121
BPHE201
BSER211
BASN310
BASN329
BTRP330
BTYR333
BHOH2021

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

246333

PDB entries from 2025-12-17

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