Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With 2'(3')-O-(N-methylanthraniloyl)-guanosine 5'-triphosphate and Mn. Determined by X-ray diffraction at 2.8 Å resolution. Released 14 Dec 2004.
Explore 1TL7 in 3D Show helices and sheets RCSB PDB PDBe
1TL7 contains 30 α-helices and 25 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 383-397 | 15 | 1 |
| α-helix | 400-404 | 5 | |
| α-helix | 409-429 | 21 | |
| β-strand | 434-438 | 5 | 1 |
| β-strand | 441-446 | 6 | 1 |
| α-helix | 455-472 | 18 | |
| α-helix | 474-477 | 4 | |
| β-strand | 483-496 | 14 | 1 |
| β-strand | 505-507 | 3 | 1 |
| α-helix | 509-519 | 11 | |
| β-strand | 526-528 | 3 | 1 |
| α-helix | 530-534 | 5 | |
| β-strand | 544 | 1 | 2 |
| α-helix | 547-549 | 3 | |
| α-helix | 552-556 | 5 | |
| β-strand | 562 | 1 | 2 |
| β-strand | 564 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 881-891 | 11 | 3 |
| α-helix | 894-898 | 5 | |
| α-helix | 909-926 | 18 | |
| β-strand | 934-940 | 7 | 3 |
| β-strand | 943-948 | 6 | 3 |
| α-helix | 967-990 | 24 | |
| β-strand | 997-1010 | 14 | 3 |
| β-strand | 1016-1020 | 5 | 3 |
| α-helix | 1022-1032 | 11 | |
| β-strand | 1039-1042 | 4 | 3 |
| α-helix | 1043-1051 | 9 | |
| β-strand | 1055-1064 | 10 | 3 |
| β-strand | 1068-1076 | 9 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 40-47 | 8 | 4 |
| α-helix | 53-64 | 12 | |
| α-helix | 90-112 | 23 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 144-155 | 12 | |
| α-helix | 157-163 | 7 | |
| α-helix | 166-168 | 3 | |
| α-helix | 175-179 | 5 | |
| α-helix | 182-186 | 5 | |
| α-helix | 194-199 | 6 | |
| β-strand | 208-214 | 7 | 4 |
| β-strand | 217-223 | 7 | 4 |
| α-helix | 231-237 | 7 | |
| β-strand | 243-249 | 7 | 4 |
| α-helix | 252-254 | 3 | |
| β-strand | 256 | 1 | 5 |
| β-strand | 264 | 1 | 5 |
| α-helix | 265-277 | 13 | |
| β-strand | 287-292 | 6 | 4 |
| α-helix | 294-303 | 10 | |
| α-helix | 313-316 | 4 | |
| α-helix | 332-350 | 19 | |
| β-strand | 359-363 | 5 | 4 |
| α-helix | 369-385 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Adenylate cyclase, type V | A | protein | 217 | Canis lupus familiaris | P30803 (AlphaFold model) |
| Adenylate cyclase, type II | B | protein | 212 | Rattus norvegicus | P26769 (AlphaFold model) |
| Guanine nucleotide-binding protein G(s), alpha subunit | C | protein | 402 | Bos taurus | P04896 (AlphaFold model) |
>1TL7_1 Adenylate cyclase, type V (chains A) MEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARF DKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREMTGVNVNM RVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVE PGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK
>1TL7_2 Adenylate cyclase, type II (chains B) RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR
>1TL7_3 Guanine nucleotide-binding protein G(s), alpha subunit (chains C) MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM RILHVNGFNGGEGGEEDPNAKSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELLGGHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| GSP | 5'-guanosine-diphosphate-monothiophosphate | C10 H16 N5 O13 P3 S | 1 |
| MG | Magnesium ion | Mg | 1 |
| ONM | 3'-O-(N-methylanthraniloyl)-guanosine-5'-triphosphate | C18 H23 N6 O15 P3 | 1 |
| FOK | Forskolin | C22 H34 O7 | 1 |
| MN | Manganese (II) ion | Mn | 2 |
Water and common crystallization additives (CL) are not listed.
Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate. Mou, T.C., Gille, A., Fancy, D.A. et al. J Biol Chem (2005) 280:7253-7261. DOI 10.1074/jbc.M409076200 · PubMed
Other PDB entries of the same protein (UniProt P30803 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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