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6R4O

Structure of a truncated adenylyl cyclase bound to MANT-GTP, forskolin and an activated stimulatory Galphas 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 Residues18
Detailsbinding site for residue ONM A 2000
ChainResidue
AASP399
AGLY442
AASP443
AMET1116
ATRP1188
AGLY1189
AASP1190
AASN1193
AMN2002
AMN2003
AILE400
AVAL401
AGLY402
APHE403
ATHR404
ASER407
ALEU415
ALEU441

site_idAC2
Number of Residues5
Detailsbinding site for residue FOK A 2001
ChainResidue
ASER511
AASN515
AASN518
AILE1111
AALA1113

site_idAC3
Number of Residues3
Detailsbinding site for residue MN A 2002
ChainResidue
AASP399
AASP443
AONM2000

site_idAC4
Number of Residues4
Detailsbinding site for residue MN A 2003
ChainResidue
AASP399
AILE400
AVAL401
AONM2000

site_idAC5
Number of Residues22
Detailsbinding site for residue GSP B 501
ChainResidue
BALA48
BGLY49
BGLU50
BSER51
BGLY52
BLYS53
BSER54
BTHR55
BLEU198
BARG199
BCYS200
BARG201
BVAL202
BTHR204
BVAL224
BGLY225
BASN292
BLYS293
BLEU296
BCYS365
BALA366
BMG502

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BSER54
BTHR204
BASP223
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
BLEU197
BASP223
BASN292
BALA366

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
BTHR204

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
BSER352

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
BLYS300

222036

PDB entries from 2024-07-03

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