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6VU5

Structure of G-alpha-q bound to its chaperone Ric-8A

Functional Information from GO Data
ChainGOidnamespacecontents
B0001508biological_processaction potential
B0001664molecular_functionG protein-coupled receptor binding
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005096molecular_functionGTPase activator activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005794cellular_componentGolgi apparatus
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0006469biological_processnegative regulation of protein kinase activity
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007202biological_processobsolete activation of phospholipase C activity
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007215biological_processglutamate receptor signaling pathway
B0007596biological_processblood coagulation
B0007603biological_processphototransduction, visible light
B0009649biological_processentrainment of circadian clock
B0010543biological_processregulation of platelet activation
B0016020cellular_componentmembrane
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0031965cellular_componentnuclear membrane
B0045202cellular_componentsynapse
B0046872molecular_functionmetal ion binding
B0050821biological_processprotein stabilization
B0060158biological_processphospholipase C-activating dopamine receptor signaling pathway
B0060828biological_processregulation of canonical Wnt signaling pathway
B0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9NPQ8
ChainResidueDetails
ASEP435

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9NPQ8
ChainResidueDetails
ATPO440
BLEU180
BTHR186
BASN274
BALA331

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3TIR3
ChainResidueDetails
ATHR442

site_idSWS_FT_FI4
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P21279
ChainResidueDetails
BCYS9
BCYS10

222926

PDB entries from 2024-07-24

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