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8SL4

Dimeric form of human adenylyl cyclase 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001973biological_processG protein-coupled adenosine receptor signaling pathway
A0004016molecular_functionadenylate cyclase activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006171biological_processcAMP biosynthetic process
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
A0007204biological_processpositive regulation of cytosolic calcium ion concentration
A0007626biological_processlocomotory behavior
A0008179molecular_functionadenylate cyclase binding
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0050885biological_processneuromuscular process controlling balance
A0061178biological_processregulation of insulin secretion involved in cellular response to glucose stimulus
A0097110molecular_functionscaffold protein binding
A1904322biological_processcellular response to forskolin
B0001973biological_processG protein-coupled adenosine receptor signaling pathway
B0004016molecular_functionadenylate cyclase activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0006171biological_processcAMP biosynthetic process
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B0007195biological_processadenylate cyclase-inhibiting dopamine receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0007626biological_processlocomotory behavior
B0008179molecular_functionadenylate cyclase binding
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
B0050885biological_processneuromuscular process controlling balance
B0061178biological_processregulation of insulin secretion involved in cellular response to glucose stimulus
B0097110molecular_functionscaffold protein binding
B1904322biological_processcellular response to forskolin
Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVL.GlrkwqFdVWSNDVTlanhmE
ChainResidueDetails
AGLY573-GLU596
AGLY1187-ASP1210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1648
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-SER195
ACYS395-SER769
AALA1005-SER1261
BMET1-SER195
BCYS395-SER769
BALA1005-SER1261

site_idSWS_FT_FI2
Number of Residues480
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLY196-PHE216
APHE910-ILE930
ALEU935-PHE955
AVAL984-HIS1004
BGLY196-PHE216
BLEU242-ALA262
BLEU268-CYS288
BGLY299-LEU319
BALA325-VAL345
BPHE374-VAL394
BLEU770-LEU790
ALEU242-ALA262
BPHE792-CYS812
BLEU836-CYS856
BPHE910-ILE930
BLEU935-PHE955
BVAL984-HIS1004
ALEU268-CYS288
AGLY299-LEU319
AALA325-VAL345
APHE374-VAL394
ALEU770-LEU790
APHE792-CYS812
ALEU836-CYS856

site_idSWS_FT_FI3
Number of Residues104
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AASN857-TYR909
BASN857-TYR909

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00099
ChainResidueDetails
AASP474
AILE475
AASP518
BASP474
BILE475
BASP518

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30803
ChainResidueDetails
ALEU516
AARG562
BLEU516
BARG562

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P26769
ChainResidueDetails
ALYS1123
AASP1197
AASN1204
ALYS1244
BLYS1123
BASP1197
BASN1204
BLYS1244

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P84309
ChainResidueDetails
AARG23
BARG23

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84309
ChainResidueDetails
ASER96
ASER155
BSER96
BSER155

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O43306
ChainResidueDetails
ASER666
BSER666

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q03343
ChainResidueDetails
ASER754
BSER754

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q03343
ChainResidueDetails
ATHR1011
BTHR1011

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN870
AASN887
BASN870
BASN887

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PDB entries from 2024-07-10

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