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4UG2

Thermostabilised HUMAN A2a Receptor with CGS21680 bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0001609molecular_functionG protein-coupled adenosine receptor activity
A0001973biological_processG protein-coupled adenosine receptor signaling pathway
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0001609molecular_functionG protein-coupled adenosine receptor activity
B0001973biological_processG protein-coupled adenosine receptor signaling pathway
B0004930molecular_functionG protein-coupled receptor activity
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLB A 1310
ChainResidue
ATRP143
AASN144
AASN145
APRO173
AASN175
BARG111
BLEU115

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NGI A 1311
ChainResidue
ALEU85
ATHR88
APHE168
AGLU169
AMET177
AASN181
ATRP246
ALEU249
AHIS250
AASN253
AHIS264
ALEU267
AMET270
AILE274
ASER277
AHIS278
AHOH2002
ASER67
AVAL84

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLB B 1306
ChainResidue
AILE108
BTRP143
BASN144
BASN145
BTYR179

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NGI B 1307
ChainResidue
BSER67
BVAL84
BLEU85
BTHR88
BPHE168
BGLU169
BMET177
BASN181
BTRP246
BLEU249
BHIS250
BASN253
BHIS264
BLEU267
BMET270
BSER277
BHIS278
BHOH2003

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSIfSLLAIAIDRYIaI
ChainResidueDetails
ASER90-ILE106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues56
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues63
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21593763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YDO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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