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3VG9

Crystal structure of human adenosine A2A receptor with an allosteric inverse-agonist antibody at 2.7 A resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ZMA A 401
ChainResidue
ALEU85
APHE168
AGLU169
ATRP246
ALEU249
AHIS250
AASN253
AMET270
ATYR271

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE STE A 402
ChainResidue
ATYR103
ALEU191
ALMT408

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE STE A 403
ChainResidue
ALEU247
ATYR290
AARG291
AHOH328
ASTE404
ASTE407

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE STE A 404
ChainResidue
ALEU190
ALEU191
ALEU194
AALA243
AARG291
ASTE403
ASTE407

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE STE A 405
ChainResidue
ACYS28
ATRP32
ATYR43
ASTE406

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE STE A 406
ChainResidue
ATRP129
ASTE405

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE STE A 407
ChainResidue
ALEU202
ALEU247
ASTE403
ASTE404

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LMT A 408
ChainResidue
ATYR179
AARG199
AARG206
ASTE402

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

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
BTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues63
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues17
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21593763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YDO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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