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5UVI

Serial Millisecond Crystallography of Membrane and Soluble Protein Micro-crystals using Synchrotron Radiation

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 Residues9
Detailsbinding site for residue ZMA A 1201
ChainResidue
APHE168
AGLU169
AMET177
ATRP246
ALEU249
AHIS250
AASN253
ALEU267
AMET270

site_idAC2
Number of Residues4
Detailsbinding site for residue CLR A 1202
ChainResidue
APHE255
APHE258
ACYS259
ACLR1204

site_idAC3
Number of Residues4
Detailsbinding site for residue CLR A 1203
ChainResidue
AILE251
ACYS262
ASER263
AALA265

site_idAC4
Number of Residues6
Detailsbinding site for residue CLR A 1204
ChainResidue
ALEU58
AALA72
AALA73
AGLY76
AILE80
ACLR1202

site_idAC5
Number of Residues2
Detailsbinding site for residue OLC A 1205
ChainResidue
AILE125
ATRP129

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 1206
ChainResidue
ASER6
ATYR271

site_idAC7
Number of Residues2
Detailsbinding site for residue OLA A 1207
ChainResidue
ASER7
ATHR11

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

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