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3C14

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate 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
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
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 Residues10
DetailsBINDING SITE FOR RESIDUE FOK A 101
ChainResidue
APHE394
BSER942
AVAL506
ATRP507
ASER508
AVAL511
ATHR512
AASN515
BPHE895
BGLY941

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE POP A 1
ChainResidue
ACA29
AASP396
AILE397
AGLU398
AGLY399
APHE400
ATHR401
AARG484
BLYS1065

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 29
ChainResidue
APOP1
AASP396
AILE397
AASP440

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 403
ChainResidue
CSER54
CTHR204
CGSP405

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 404
ChainResidue
CALA249
CHOH406

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GSP C 405
ChainResidue
CGLU50
CSER51
CGLY52
CLYS53
CSER54
CTHR55
CASP173
CLEU198
CARG199
CARG201
CTHR204
CVAL224
CGLY225
CGLY226
CASN292
CLYS293
CASP295
CLEU296
CCYS365
CALA366
CVAL367
CMG403

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 Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641
ChainResidueDetails
CASN292
CALA366
CGLY47
CLEU197
CASP223

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715
ChainResidueDetails
CSER54
CTHR204

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
CSER352

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119
ChainResidueDetails
CGLY2

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119
ChainResidueDetails
CCYS3

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
CLYS300

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

221051

PDB entries from 2024-06-12

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