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7TMW

Cryo-EM structure of the relaxin receptor RXFP1 in complex with heterotrimeric Gs

Functional Information from GO Data
ChainGOidnamespacecontents
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
C0005515molecular_functionprotein binding
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
C0016020cellular_componentmembrane
C0031681molecular_functionG-protein beta-subunit binding
C0048144biological_processfibroblast proliferation
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
R0003924molecular_functionGTPase activity
R0004930molecular_functionG protein-coupled receptor activity
R0005515molecular_functionprotein binding
R0005525molecular_functionGTP binding
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007567biological_processparturition
R0008528molecular_functionG protein-coupled peptide receptor activity
R0009755biological_processhormone-mediated signaling pathway
R0016020cellular_componentmembrane
R0019001molecular_functionguanyl nucleotide binding
R0030198biological_processextracellular matrix organization
R0031683molecular_functionG-protein beta/gamma-subunit complex binding
R0036446biological_processmyofibroblast differentiation
R0042562molecular_functionhormone binding
R0046872molecular_functionmetal ion binding
R0060427biological_processlung connective tissue development
R0060658biological_processnipple morphogenesis
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU80-SER94
BILE167-ILE181
BLEU295-ALA309

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CLpqllh.CNgvdDCgnqaDEDn....C
ChainResidueDetails
RCYS40-CYS62

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
CALA2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
CCYS68
RLEU508-ARG527
RTYR599-ARG629

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
CCYS68

site_idSWS_FT_FI4
Number of Residues50
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RASP465-GLN486
RASN549-GLN577
RSER651

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RLEU487-THR507

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RTHR528-SER548

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RILE578-SER598

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RPHE630-LEU650

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RLEU652-ILE672

site_idSWS_FT_FI10
Number of Residues6
DetailsBINDING:
ChainResidueDetails
RLEU45
RASN48
RVAL50
RASP52
RASP58
RGLU59

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18533687
ChainResidueDetails
RASN36
RASN127
RASN264
RASN272
RASN325
RASN368

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04896
ChainResidueDetails
RTHR1199
RASP1218
RLEU1287
RPHE1361

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
RHIS1347

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
RASP1295

222624

PDB entries from 2024-07-17

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