Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5VRA

2.35-Angstrom In situ Mylar structure of human A2A adenosine receptor at 100 K

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
A0005506molecular_functioniron ion binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue ZMA A 2401
ChainResidue
APHE168
AILE274
AHOH2531
AHOH2552
AHOH2563
AGLU169
AMET177
ATRP246
ALEU249
AHIS250
AASN253
ALEU267
AMET270

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 2402
ChainResidue
AASP52
ASER91
AHOH2530
AHOH2561
AHOH2576

site_idAC3
Number of Residues4
Detailsbinding site for residue CLR A 2403
ChainResidue
APRO248
ACYS262
ASER263
AOLA2412

site_idAC4
Number of Residues3
Detailsbinding site for residue CLR A 2404
ChainResidue
APHE258
AOLC2407
AOLA2412

site_idAC5
Number of Residues7
Detailsbinding site for residue CLR A 2405
ChainResidue
AALA72
AALA73
AGLY76
AILE80
AOLC2406
AOLC2407
AOLC2408

site_idAC6
Number of Residues4
Detailsbinding site for residue OLC A 2406
ChainResidue
APHE258
ACLR2405
AOLC2409
AOLC2410

site_idAC7
Number of Residues8
Detailsbinding site for residue OLC A 2407
ChainResidue
ALEU58
APRO61
ATHR65
APHE70
ACLR2404
ACLR2405
AOLA2412
AOLA2413

site_idAC8
Number of Residues5
Detailsbinding site for residue OLC A 2408
ChainResidue
ATYR43
AVAL46
ALEU58
ATRP129
ACLR2405

site_idAC9
Number of Residues2
Detailsbinding site for residue OLC A 2409
ChainResidue
AMET140
AOLC2406

site_idAD1
Number of Residues3
Detailsbinding site for residue OLC A 2410
ChainResidue
ATYR179
APHE258
AOLC2406

site_idAD2
Number of Residues4
Detailsbinding site for residue OLC A 2411
ChainResidue
AHIS75
AMET140
ALEU141
ATYR179

site_idAD3
Number of Residues7
Detailsbinding site for residue OLA A 2412
ChainResidue
APHE255
ACYS262
ACLR2403
ACLR2404
AOLC2407
AOLA2414
AHOH2566

site_idAD4
Number of Residues4
Detailsbinding site for residue OLA A 2413
ChainResidue
APHE70
AOLC2407
AOLA2414
AOLA2415

site_idAD5
Number of Residues3
Detailsbinding site for residue OLA A 2414
ChainResidue
AOLA2412
AOLA2413
AOLA2415

site_idAD6
Number of Residues3
Detailsbinding site for residue OLA A 2415
ChainResidue
AILE10
AOLA2413
AOLA2414

site_idAD7
Number of Residues1
Detailsbinding site for residue OLA A 2416
ChainResidue
AHIS264

site_idAD8
Number of Residues4
Detailsbinding site for residue OLA A 2417
ChainResidue
AGLY5
ASER6
ATYR271
AVAL275

site_idAD9
Number of Residues1
Detailsbinding site for residue OLA A 2418
ChainResidue
AALA97

site_idAE1
Number of Residues2
Detailsbinding site for residue OLA A 2419
ChainResidue
ATHR279
APHE286

site_idAE2
Number of Residues4
Detailsbinding site for residue OLA A 2420
ChainResidue
ALEU19
ALEU22
ATRP29
APHE286

site_idAE3
Number of Residues4
Detailsbinding site for residue OLB A 2422
ChainResidue
AVAL31
ATRP32
AALA50
AARG205

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 Residues24
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AVAL8-TRP32

site_idSWS_FT_FI2
Number of Residues28
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18832607
ChainResidueDetails
ALEU33-ASN42
AASP101-ARG120

site_idSWS_FT_FI3
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ATYR43-ILE66

site_idSWS_FT_FI4
Number of Residues46
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18832607
ChainResidueDetails
ASER67-CYS77
AASN144-PRO173
ACYS259-PRO266

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ALEU78-ILE100

site_idSWS_FT_FI6
Number of Residues22
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AALA121-TRP143

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AMET174-LEU198

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ALEU235-PHE258

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
ALEU267-TYR290

site_idSWS_FT_FI10
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21593763, ECO:0007744|PDB:2YDO
ChainResidueDetails
AGLU169
AASN253
ASER277
AHIS278

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN154

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon