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8HPT

Structure of C5a-pep bound mouse C5aR1 in complex with Go

Functional Information from GO Data
ChainGOidnamespacecontents
A0001774biological_processmicroglial cell activation
A0002684biological_processpositive regulation of immune system process
A0004875molecular_functioncomplement receptor activity
A0004878molecular_functioncomplement component C5a receptor activity
A0004930molecular_functionG protein-coupled receptor activity
A0005886cellular_componentplasma membrane
A0006935biological_processchemotaxis
A0007186biological_processG protein-coupled receptor signaling pathway
A0010575biological_processpositive regulation of vascular endothelial growth factor production
A0010759biological_processpositive regulation of macrophage chemotaxis
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0030593biological_processneutrophil chemotaxis
A0031410cellular_componentcytoplasmic vesicle
A0032494biological_processresponse to peptidoglycan
A0038178biological_processcomplement component C5a signaling pathway
A0042789biological_processmRNA transcription by RNA polymerase II
A0045177cellular_componentapical part of cell
A0045766biological_processpositive regulation of angiogenesis
A0048143biological_processastrocyte activation
A0050679biological_processpositive regulation of epithelial cell proliferation
A0050830biological_processdefense response to Gram-positive bacterium
A0050890biological_processcognition
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0090023biological_processpositive regulation of neutrophil chemotaxis
A0097242biological_processamyloid-beta clearance
A0099172biological_processpresynapse organization
A1902947biological_processregulation of tau-protein kinase activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0001750cellular_componentphotoreceptor outer segment
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
C0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
C0007265biological_processRas protein signal transduction
C0008283biological_processcell population proliferation
C0016020cellular_componentmembrane
C0030159molecular_functionsignaling receptor complex adaptor activity
C0044877molecular_functionprotein-containing complex binding
C0045202cellular_componentsynapse
C0050909biological_processsensory perception of taste
C0051020molecular_functionGTPase binding
C0060041biological_processretina development in camera-type eye
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
C0097381cellular_componentphotoreceptor disc membrane
C1903561cellular_componentextracellular vesicle
G0005834cellular_componentheterotrimeric G-protein complex
G0007186biological_processG protein-coupled receptor signaling pathway
G0031681molecular_functionG-protein beta-subunit binding
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIlLLATISADRFLlV
ChainResidueDetails
AALA122-VAL138

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
CLEU70-SER84
CILE157-ILE171
CLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphohistidine => ECO:0000250|UniProtKB:P62871
ChainResidueDetails
CHIS266
BLYS46
BSER47
BTHR48
BTHR182
BLYS280
BPRO283
BILE335

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: 5-glutamyl histamine => ECO:0000250|UniProtKB:P18872
ChainResidueDetails
BGLN205
AASP133-ALA153
ALEU228-LYS243
AGLY305-VAL351

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
AVAL70-PHE93

site_idSWS_FT_FI4
Number of Residues58
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
ATHR94-ILE110
AARG175-LYS201
AALA267-ASN283

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
AVAL111-ALA132

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
ATRP154-TYR174

site_idSWS_FT_FI7
Number of Residues25
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
AALA202-LEU227

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
AVAL244-ILE266

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
ASER284-ALA304

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
ATYR13
ATYR16

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21730
ChainResidueDetails
ASER315
ASER318
ASER328
ASER339

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER325

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19144319
ChainResidueDetails
ASER333

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN6

225946

PDB entries from 2024-10-09

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