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6R4P

Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0004016molecular_functionadenylate cyclase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006091biological_processgeneration of precursor metabolites and energy
A0006171biological_processcAMP biosynthetic process
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0008218biological_processbioluminescence
A0009190biological_processcyclic nucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
A0046872molecular_functionmetal ion binding
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue GSP B 501
ChainResidue
BGLY49
BARG201
BTHR204
BGLY226
BASN292
BLYS293
BASP295
BLEU296
BCYS365
BALA366
BVAL367
BGLU50
BMG502
BSER51
BGLY52
BLYS53
BSER54
BTHR55
BLEU198
BARG199

site_idAC2
Number of Residues3
Detailsbinding site for residue MG B 502
ChainResidue
BSER54
BTHR204
BGSP501

Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GIL.GmrrfkFdVWSNDVNlanlmE
ChainResidueDetails
AGLY498-GLU521
AGLY1176-ASP1199

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
BGLY47
BLEU198
BVAL224
BLYS293
BVAL367

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
BSER54
BSER205

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
BGLY353

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119
ChainResidueDetails
BGLY2

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119
ChainResidueDetails
BCYS3

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
BVAL301

222036

PDB entries from 2024-07-03

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