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6JZH

Structure of human A2A adenosine receptor in complex with ZM241385 obtained from SFX experiments under atmospheric pressure

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 Residues5
Detailsbinding site for residue NA A 2001
ChainResidue
AASP52
ASER91
AHOH2118
AHOH2138
AHOH2150

site_idAC2
Number of Residues12
Detailsbinding site for residue ZMA A 2002
ChainResidue
ATRP246
ALEU249
AHIS250
AASN253
AMET270
AHOH2133
AHOH2143
AHOH2147
ALEU85
APHE168
AGLU169
AMET177

site_idAC3
Number of Residues2
Detailsbinding site for residue OLA A 2003
ChainResidue
ATHR65
APHE70

site_idAC4
Number of Residues2
Detailsbinding site for residue OLA A 2005
ChainResidue
ASER7
ATHR11

site_idAC5
Number of Residues1
Detailsbinding site for residue OLA A 2006
ChainResidue
APRO266

site_idAC6
Number of Residues2
Detailsbinding site for residue OLA A 2007
ChainResidue
AOLA2020
ACLR2023

site_idAC7
Number of Residues1
Detailsbinding site for residue OLA A 2008
ChainResidue
ACLR2022

site_idAC8
Number of Residues1
Detailsbinding site for residue OLA A 2009
ChainResidue
ATYR179

site_idAC9
Number of Residues3
Detailsbinding site for residue OLA A 2010
ChainResidue
AALA50
ALYS122
ATRP129

site_idAD1
Number of Residues2
Detailsbinding site for residue OLA A 2011
ChainResidue
ACYS28
ALEU58

site_idAD2
Number of Residues1
Detailsbinding site for residue OLA A 2012
ChainResidue
ATYR179

site_idAD3
Number of Residues3
Detailsbinding site for residue OLA A 2013
ChainResidue
ATYR290
AOLA2014
AHOH2149

site_idAD4
Number of Residues5
Detailsbinding site for residue OLA A 2014
ChainResidue
AGLY5
ASER6
ALEU267
ATYR271
AOLA2013

site_idAD5
Number of Residues1
Detailsbinding site for residue OLA A 2015
ChainResidue
ATRP268

site_idAD6
Number of Residues2
Detailsbinding site for residue OLA A 2016
ChainResidue
ASER7
APHE286

site_idAD7
Number of Residues4
Detailsbinding site for residue OLA A 2017
ChainResidue
ATRP32
APHE201
ALYS233
AOLA2018

site_idAD8
Number of Residues3
Detailsbinding site for residue OLA A 2018
ChainResidue
ATRP29
ATRP32
AOLA2017

site_idAD9
Number of Residues2
Detailsbinding site for residue OLA A 2019
ChainResidue
ASER6
ATHR68

site_idAE1
Number of Residues5
Detailsbinding site for residue OLA A 2020
ChainResidue
ATHR65
ACYS71
AOLA2007
ACLR2022
ACLR2024

site_idAE2
Number of Residues2
Detailsbinding site for residue OLA A 2021
ChainResidue
AALA73
AGLY76

site_idAE3
Number of Residues6
Detailsbinding site for residue CLR A 2022
ChainResidue
AALA72
AALA73
AILE80
AOLA2008
AOLA2020
ACLR2024

site_idAE4
Number of Residues3
Detailsbinding site for residue CLR A 2023
ChainResidue
ACYS262
ASER263
AOLA2007

site_idAE5
Number of Residues7
Detailsbinding site for residue CLR A 2024
ChainResidue
ALEU187
APHE255
APHE258
ACYS259
AOLA2020
ACLR2022
AHOH2106

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
AGLN154

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

222926

PDB entries from 2024-07-24

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