7PDE
Structure of Adenylyl cyclase 9 in complex with Gs protein alpha subunit and MANT-GTP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001701 | biological_process | in utero embryonic development |
A | 0004016 | molecular_function | adenylate cyclase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006171 | biological_process | cAMP biosynthetic process |
A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016829 | molecular_function | lyase activity |
A | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
A | 0035556 | biological_process | intracellular signal transduction |
A | 0046872 | molecular_function | metal ion binding |
A | 0071880 | biological_process | adenylate cyclase-activating adrenergic receptor signaling pathway |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0007165 | biological_process | signal transduction |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0019001 | molecular_function | guanyl nucleotide binding |
B | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
Functional Information from PROSITE/UniProt
site_id | PS00452 |
Number of Residues | 24 |
Details | GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GIL.GmrrfkFdVWSNDVNlanlmE |
Chain | Residue | Details |
A | GLY498-GLU521 | |
A | GLY1176-ASP1199 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: 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 |
Chain | Residue | Details |
B | GLY47 | |
B | LEU197 | |
B | ASP223 | |
B | ASN292 | |
B | ALA366 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: 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 |
Chain | Residue | Details |
B | SER54 | |
B | THR204 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092 |
Chain | Residue | Details |
B | SER352 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | LIPID: N-palmitoyl glycine => ECO:0000269|PubMed:12574119 |
Chain | Residue | Details |
B | GLY2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:12574119 |
Chain | Residue | Details |
B | CYS3 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092 |
Chain | Residue | Details |
B | LYS300 |