Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg. Determined by X-ray diffraction at 2.78 Å resolution. Released 3 Feb 2009.
Explore 3C15 in 3D Show helices and sheets RCSB PDB PDBe
3C15 contains 35 α-helices and 28 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 |
|---|---|---|---|
| α-helix | 380-382 | 3 | |
| β-strand | 383-398 | 16 | 1 |
| α-helix | 400-406 | 7 | |
| α-helix | 409-429 | 21 | |
| β-strand | 432-438 | 7 | 1 |
| β-strand | 441-446 | 6 | 1 |
| α-helix | 455-475 | 21 | |
| β-strand | 482-496 | 15 | 1 |
| β-strand | 505-507 | 3 | 1 |
| α-helix | 509-519 | 11 | |
| β-strand | 526-528 | 3 | 1 |
| α-helix | 531-534 | 4 | |
| β-strand | 542-544 | 3 | 1 |
| α-helix | 547-549 | 3 | |
| α-helix | 552-556 | 5 | |
| β-strand | 562-564 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 880-881 | 2 | 2 |
| β-strand | 885 | 1 | 3 |
| β-strand | 886-891 | 6 | 4 |
| α-helix | 894-898 | 5 | |
| α-helix | 909-923 | 15 | |
| α-helix | 929-931 | 3 | |
| β-strand | 934-939 | 6 | 4 |
| β-strand | 943-948 | 6 | 4 |
| α-helix | 967-990 | 24 | |
| α-helix | 994-996 | 3 | |
| β-strand | 997-1000 | 4 | 4 |
| β-strand | 1003 | 1 | 3 |
| β-strand | 1006-1010 | 5 | 2 |
| β-strand | 1016-1020 | 5 | 2 |
| α-helix | 1022-1032 | 11 | |
| β-strand | 1039-1042 | 4 | 4 |
| α-helix | 1043-1050 | 8 | |
| β-strand | 1056-1064 | 9 | 4 |
| β-strand | 1068-1075 | 8 | 4 |
| α-helix | 1076 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 42-47 | 6 | 5 |
| α-helix | 53-64 | 12 | |
| α-helix | 89-112 | 24 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-134 | 10 | |
| α-helix | 144-155 | 12 | |
| α-helix | 157-164 | 8 | |
| 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 | 5 |
| β-strand | 217-223 | 7 | 5 |
| α-helix | 231-237 | 7 | |
| β-strand | 243-249 | 7 | 5 |
| α-helix | 250-254 | 5 | |
| β-strand | 256 | 1 | 6 |
| β-strand | 264 | 1 | 6 |
| α-helix | 265-277 | 13 | |
| β-strand | 287-292 | 6 | 5 |
| α-helix | 294-303 | 10 | |
| α-helix | 308-310 | 3 | |
| α-helix | 313-316 | 4 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-350 | 19 | |
| β-strand | 359-363 | 5 | 5 |
| α-helix | 369-386 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Adenylate cyclase type 5 | A | protein | 225 | Canis lupus familiaris | P30803 (AlphaFold model) |
| Adenylate cyclase type 2 | B | protein | 212 | Rattus norvegicus | P26769 (AlphaFold model) |
| Guanine nucleotide-binding protein G(s) subunit alpha isoforms short | C | protein | 402 | Bos taurus | P04896 (AlphaFold model) |
>3C15_1 Adenylate cyclase type 5 (chains A) MHHHHHHAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMT LNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVRE MTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSY LNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAK
>3C15_2 Adenylate cyclase type 2 (chains B) RSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKP KFSGVEKIKTIGSTYMAATGLSAIPSQEHAQEPERQYMHIGTMVEFAYALVGKLDAINKH SFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLIL QTLGYTCTCRGIINVKGKGDLKTYFVNTEMSR
>3C15_3 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains C) MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD KIDVIKQDDYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELLGGHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| FOK | Forskolin | C22 H34 O7 | 1 |
| GSP | 5'-guanosine-diphosphate-monothiophosphate | C10 H16 N5 O13 P3 S | 1 |
| POP | Pyrophosphate 2- | H2 O7 P2 | 1 |
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (CL) are not listed.
Structural basis for inhibition of mammalian adenylyl cyclase by calcium. Mou, T.C., Masada, N., Cooper, D.M. et al. Biochemistry (2009) 48:3387-3397. DOI 10.1021/bi802122k · 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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