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9U3P

Cryo-EM structure of human AC9-Gs complex (soluble domain)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001701biological_processin utero embryonic development
A0003091biological_processrenal water homeostasis
A0004016molecular_functionadenylate cyclase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006171biological_processcAMP biosynthetic process
A0007165biological_processsignal transduction
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0036064cellular_componentciliary basal body
A0046872molecular_functionmetal ion binding
A0071377biological_processcellular response to glucagon stimulus
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
A0097700biological_processvascular endothelial cell response to laminar fluid shear stress
B0000166molecular_functionnucleotide binding
B0001678biological_processintracellular glucose homeostasis
B0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
B0003091biological_processrenal water homeostasis
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007190biological_processactivation of adenylate cyclase activity
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007192biological_processadenylate cyclase-activating serotonin receptor signaling pathway
B0007608biological_processsensory perception of smell
B0010856molecular_functionadenylate cyclase activator activity
B0014819biological_processregulation of skeletal muscle contraction
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0031748molecular_functionD1 dopamine receptor binding
B0032024biological_processpositive regulation of insulin secretion
B0032588cellular_componenttrans-Golgi network membrane
B0034695biological_processresponse to prostaglandin E
B0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
B0038184biological_processadenylate cyclase-activating G protein-coupled bile acid receptor signaling pathway
B0046872molecular_functionmetal ion binding
B0046907biological_processintracellular transport
B0048589biological_processdevelopmental growth
B0050890biological_processcognition
B0060348biological_processbone development
B0060789biological_processhair follicle placode formation
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B0071377biological_processcellular response to glucagon stimulus
B0071380biological_processcellular response to prostaglandin E stimulus
B0071468biological_processcellular response to acidic pH
B0071870biological_processcellular response to catecholamine stimulus
B0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
B0097700biological_processvascular endothelial cell response to laminar fluid shear stress
B0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GIL.GmrrfkFdVWSNDVNlanlmE
ChainResidueDetails
AGLY498-GLU521
AGLY1175-ASP1198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues127
DetailsDomain: {"description":"Guanylate cyclase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues140
DetailsDomain: {"description":"Guanylate cyclase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30803","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P26769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues25
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04896","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine; by cholera toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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