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7VUJ

Cryo-EM structure of a class A orphan GPCR

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
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
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0048144biological_processfibroblast proliferation
G0070062cellular_componentextracellular exosome
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
R0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
R0004930molecular_functionG protein-coupled receptor activity
R0005886cellular_componentplasma membrane
R0007186biological_processG protein-coupled receptor signaling pathway
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0007218biological_processneuropeptide signaling pathway
R0008188molecular_functionneuropeptide receptor activity
R0016020cellular_componentmembrane
R0016798molecular_functionhydrolase activity, acting on glycosyl bonds
R0031176molecular_functionendo-1,4-beta-xylanase activity
R0042802molecular_functionidentical protein binding
R0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
ChainResidueDetails
RPRO-109-TRP-99

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
RMET-15-SER-4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04896
ChainResidueDetails
AGLY47
ASER54
ATHR204
AASP223
ALEU292
APHE366

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AHIS352

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
AASP300

site_idSWS_FT_FI4
Number of Residues63
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
RLEU51-TYR65
RILE124-VAL148
RASN203-ALA228

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
RLEU66-LEU86

site_idSWS_FT_FI6
Number of Residues44
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RLEU87-LYS102
RTRP170-HIS181
RTYR250-ASP268

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RILE103-THR123

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RILE149-ILE169

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RVAL182-LEU202

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RILE229-LEU249

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RILE269-SER289

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN11

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
RASN-149modifies pKa
RTYR-115electrostatic destabiliser
RGLU-106covalent catalysis, proton shuttle (general acid/base)
RTYR-104modifies pKa
RGLU-12proton shuttle (general acid/base)

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PDB entries from 2024-07-24

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