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9IPY

Structure of JR14a-bound human C3aR

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
R0002430biological_processcomplement receptor mediated signaling pathway
R0002684biological_processpositive regulation of immune system process
R0004876molecular_functioncomplement component C3a receptor activity
R0004878molecular_functioncomplement component C5a receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0005886cellular_componentplasma membrane
R0006935biological_processchemotaxis
R0006954biological_processinflammatory response
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0007204biological_processpositive regulation of cytosolic calcium ion concentration
R0008015biological_processblood circulation
R0010575biological_processpositive regulation of vascular endothelial growth factor production
R0010759biological_processpositive regulation of macrophage chemotaxis
R0016020cellular_componentmembrane
R0019722biological_processcalcium-mediated signaling
R0035577cellular_componentazurophil granule membrane
R0035579cellular_componentspecific granule membrane
R0038178biological_processcomplement component C5a signaling pathway
R0045766biological_processpositive regulation of angiogenesis
R0090023biological_processpositive regulation of neutrophil chemotaxis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVfLLTAISLDRCLvV
ChainResidueDetails
RALA108-VAL124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues16
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"source":"PubMed","id":"12871936","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O09047","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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