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3C16

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine-5'-Triphosphate and Ca

Functional Information from GO Data
ChainGOidnamespacecontents
A0009190biological_processcyclic nucleotide biosynthetic process
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
B0009190biological_processcyclic nucleotide biosynthetic process
B0016849molecular_functionphosphorus-oxygen lyase activity
B0035556biological_processintracellular signal transduction
C0000166molecular_functionnucleotide binding
C0003924molecular_functionGTPase activity
C0005159molecular_functioninsulin-like growth factor receptor binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007606biological_processsensory perception of chemical stimulus
C0010856molecular_functionadenylate cyclase activator activity
C0016787molecular_functionhydrolase activity
C0019001molecular_functionguanyl nucleotide binding
C0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0031698molecular_functionbeta-2 adrenergic receptor binding
C0031748molecular_functionD1 dopamine receptor binding
C0031852molecular_functionmu-type opioid receptor binding
C0035255molecular_functionionotropic glutamate receptor binding
C0046872molecular_functionmetal ion binding
C0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
C0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 397
ChainResidue
CALA227

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 398
ChainResidue
CSER51
CTHR182
CASP201
CVAL202
CGSP395

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 29
ChainResidue
AILE397
AASP440
AATP1
ACA30
AASP396

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 30
ChainResidue
AATP1
AHOH2
ACA29
AASP396
AASP440

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GSP C 395
ChainResidue
CGLU47
CSER48
CGLY49
CLYS50
CSER51
CTHR52
CASP151
CLEU176
CARG177
CARG179
CTHR182
CGLY203
CGLY204
CASN270
CLYS271
CASP273
CLEU274
CCYS343
CALA344
CVAL345
CMG398

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FOK A 101
ChainResidue
AVAL506
ATRP507
ASER508
AVAL511
ATHR512
AASN515
BTYR899
BILE940
BGLY941
BSER942

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
AHOH4
AHOH5
AHOH6
ACA29
ACA30
AASP396
AILE397
AGLU398
APHE400
ATHR401
ALEU438
AGLY439
BASN1025
BLYS1065

Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVI.GaqkpqYdIWGNTVNvasrmD
ChainResidueDetails
BGLY1008-ASP1031
AGLY495-GLU518

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 Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsRegion: {"description":"Interaction with GNAS","evidences":[{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CJK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues23
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
BARG1029

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
AHIS516

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
CARG179
CGLU47
CTHR182
CGLN205

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ab8
ChainResidueDetails
CGLN205

site_idMCSA1
Number of Residues2
DetailsM-CSA 58
ChainResidueDetails
BARG1029electrostatic stabiliser
BLYS1065electrostatic stabiliser
AASP440metal ligand

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PDB entries from 2025-12-17

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