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

5K2B

2.5 angstrom A2a adenosine receptor structure with MR phasing using XFEL data

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 Residues12
Detailsbinding site for residue ZMA A 1201
ChainResidue
ALEU85
AHOH1325
AHOH1334
AHOH1345
APHE168
AGLU169
ATRP246
ALEU249
AHIS250
AASN253
ALEU267
AMET270

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 1202
ChainResidue
AASP52
ASER91
AHOH1327
AHOH1340
AHOH1355

site_idAC3
Number of Residues5
Detailsbinding site for residue CLR A 1203
ChainResidue
APHE255
APHE258
ACLR1205
AOLC1207
AHOH1311

site_idAC4
Number of Residues4
Detailsbinding site for residue CLR A 1204
ChainResidue
ACYS262
ASER263
AOLC1221
AHOH1301

site_idAC5
Number of Residues4
Detailsbinding site for residue CLR A 1205
ChainResidue
AALA72
AALA73
AILE80
ACLR1203

site_idAC6
Number of Residues4
Detailsbinding site for residue OLB A 1206
ChainResidue
ATHR65
APHE70
ACYS71
AOLC1221

site_idAC7
Number of Residues2
Detailsbinding site for residue OLC A 1207
ChainResidue
APHE258
ACLR1203

site_idAC8
Number of Residues4
Detailsbinding site for residue OLC A 1208
ChainResidue
ACYS28
AVAL46
AARG205
AOLC1209

site_idAC9
Number of Residues4
Detailsbinding site for residue OLC A 1209
ChainResidue
ATYR43
AILE125
ATRP129
AOLC1208

site_idAD1
Number of Residues4
Detailsbinding site for residue OLC A 1210
ChainResidue
AHIS75
AMET140
ALEU141
ATYR179

site_idAD2
Number of Residues4
Detailsbinding site for residue OLC A 1212
ChainResidue
APRO2
ASER6
AOLA1214
AOLA1215

site_idAD3
Number of Residues3
Detailsbinding site for residue OLA A 1213
ChainResidue
ASER7
ALEU19
ALEU22

site_idAD4
Number of Residues1
Detailsbinding site for residue OLA A 1214
ChainResidue
AOLC1212

site_idAD5
Number of Residues3
Detailsbinding site for residue OLA A 1215
ChainResidue
ATYR290
AOLC1212
AHOH1302

site_idAD6
Number of Residues2
Detailsbinding site for residue OLA A 1216
ChainResidue
AALA97
AILE124

site_idAD7
Number of Residues3
Detailsbinding site for residue OLA A 1217
ChainResidue
AILE10
ALEU14
AOLC1220

site_idAD8
Number of Residues1
Detailsbinding site for residue OLA A 1218
ChainResidue
ATHR11

site_idAD9
Number of Residues4
Detailsbinding site for residue OLC A 1220
ChainResidue
ATHR65
ATHR68
AOLA1217
AOLC1221

site_idAE1
Number of Residues6
Detailsbinding site for residue OLC A 1221
ChainResidue
APHE255
ACYS262
ACLR1204
AOLB1206
AOLC1220
AHOH1301

site_idAE2
Number of Residues2
Detailsbinding site for residue OLC A 1222
ChainResidue
AHIS75
AGLY76

site_idAE3
Number of Residues1
Detailsbinding site for residue OLA A 1223
ChainResidue
ALEU241

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
AASN253
ASER277
AHIS278
AGLU169

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

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon