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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: axial binding residue
ChainResidueDetails
RTRP1012
RILE1107

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
RILE24-TRP46

site_idSWS_FT_FI3
Number of Residues73
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
RVAL47-ASN57
RASP119-ALA139
RGLY439-VAL482

site_idSWS_FT_FI4
Number of Residues22
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
RTHR58-ALA80

site_idSWS_FT_FI5
Number of Residues210
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RHIS81-LYS96
RARG161-ARG340
RLEU401-ASP417

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RLEU97-LEU118

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RCYS140-TYR160

site_idSWS_FT_FI8
Number of Residues19
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RLEU341-VAL360

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RVAL378-SER400

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RHIS418-LEU438

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:12871936
ChainResidueDetails
RTYR174
RTYR184
RTYR318

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O09047
ChainResidueDetails
RSER459

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O09047
ChainResidueDetails
RTHR463

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN9
RASN194

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360
ChainResidueDetails
RSER266

238268

PDB entries from 2025-07-02

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